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Journal articles on the topic 'Ack1'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Lin, Qiong, Jian Wang, Chandra Childress, and Wannian Yang. "The activation mechanism of ACK1 (activated Cdc42-associated tyrosine kinase 1)." Biochemical Journal 445, no. 2 (June 27, 2012): 255–64. http://dx.doi.org/10.1042/bj20111575.

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ACK [activated Cdc42 (cell division cycle 42)-associated tyrosine kinase; also called TNK2 (tyrosine kinase, non-receptor, 2)] is activated in response to multiple cellular signals, including cell adhesion, growth factor receptors and heterotrimeric G-protein-coupled receptor signalling. However, the molecular mechanism underlying activation of ACK remains largely unclear. In the present study, we demonstrated that interaction of the SH3 (Src homology 3) domain with the EBD [EGFR (epidermal growth factor receptor)-binding domain] in ACK1 forms an auto-inhibition of the kinase activity. Release of this auto-inhibition is a key step for activation of ACK1. Mutation of the SH3 domain caused activation of ACK1, independent of cell adhesion, suggesting that cell adhesion-mediated activation of ACK1 is through releasing the auto-inhibition. A region at the N-terminus of ACK1 (Leu10–Leu14) is essential for cell adhesion-mediated activation. In the activation of ACK1 by EGFR signalling, Grb2 (growth-factor-receptor-bound protein 2) mediates the interaction of ACK1 with EGFR through binding to the EBD and activates ACK1 by releasing the auto-inhibition. Furthermore, we found that mutation of Ser445 to proline caused constitutive activation of ACK1. Taken together, our studies have revealed a novel molecular mechanism underlying activation of ACK1.

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2

Shen, Feng, Qiong Lin, Yan Gu, Chandra Childress, and Wannian Yang. "Activated Cdc42-associated Kinase 1 Is a Component of EGF Receptor Signaling Complex and Regulates EGF Receptor Degradation." Molecular Biology of the Cell 18, no. 3 (March 2007): 732–42. http://dx.doi.org/10.1091/mbc.e06-02-0142.

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Cdc42-associated tyrosine kinase 1 (ACK1) is a specific down-stream effector of Cdc42, a Rho family small G-protein. Previous studies have shown that ACK1 interacts with clathrin heavy chain and is involved in clathrin-coated vesicle endocytosis. Here we report that ACK1 interacted with epidermal growth factor receptor (EGFR) upon EGF stimulation via a region at carboxy terminus that is highly homologous to Gene-33/Mig-6/RALT. The interaction of ACK1 with EGFR was dependent on the kinase activity or tyrosine phosphorylation of EGFR. Immunofluorescent staining using anti-EGFR and GFP-ACK1 indicates that ACK1 was colocalized with EGFR on EEA-1 positive vesicles upon EGF stimulation. Suppression of the expression of ACK1 by ACK-RNAi inhibited ligand-induced degradation of EGFR upon EGF stimulation, suggesting that ACK1 plays an important role in regulation of EGFR degradation in cells. Furthermore, we identified ACK1 as an ubiquitin-binding protein. Through an ubiquitin-association (Uba) domain at the carboxy terminus, ACK1 binds to both poly- and mono-ubiquitin. Overexpression of the Uba domain-deletion mutant of ACK1 blocked the ligand-dependent degradation of EGFR, suggesting that ACK1 regulates EGFR degradation via its Uba domain. Taken together, our studies suggest that ACK1 senses signal of EGF and regulates ligand-induced degradation of EGFR.

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3

Prieto-Echagüe, Victoria, and W. Todd Miller. "Regulation of Ack-Family Nonreceptor Tyrosine Kinases." Journal of Signal Transduction 2011 (February 17, 2011): 1–9. http://dx.doi.org/10.1155/2011/742372.

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Ack family non-receptor tyrosine kinases are unique with regard to their domain composition and regulatory properties. Human Ack1 (activated Cdc42-associated kinase) is ubiquitously expressed and is activated by signals that include growth factors and integrin-mediated cell adhesion. Stimulation leads to Ack1 autophosphorylation and to phosphorylation of additional residues in the C-terminus. The N-terminal SAM domain is required for full activation. Ack1 exerts some of its effects via protein-protein interactions that are independent of its kinase activity. In the basal state, Ack1 activity is suppressed by an intramolecular interaction between the catalytic domain and the C-terminal region. Inappropriate Ack1 activation and signaling has been implicated in the development, progression, and metastasis of several forms of cancer. Thus, there is increasing interest in Ack1 as a drug target, and studies of the regulatory properties of the enzyme may reveal features that can be exploited in inhibitor design.

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4

Chan, Wing, Soon-Tuck Sit, and Ed Manser. "The Cdc42-associated kinase ACK1 is not autoinhibited but requires Src for activation." Biochemical Journal 435, no. 2 (March 29, 2011): 355–64. http://dx.doi.org/10.1042/bj20102156.

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The non-RTK (receptor tyrosine kinase) ACK1 [activated Cdc42 (cell division cycle 42)-associated kinase 1] binds a number of RTKs and is associated with their endocytosis and turnover. Its mode of activation is not well established, but models have suggested that this is an autoinhibited kinase. Point mutations in its SH3 (Src homology 3)- or EGF (epidermal growth factor)-binding domains have been reported to activate ACK1, but we find neither of the corresponding W424K or F820A mutations do so. Indeed, deletion of the various ACK1 domains C-terminal to the catalytic domain are not associated with increased activity. A previous report identified only one major tyrosine phosphorylated protein of 60 kDa co-purified with ACK1. In a screen for new SH3 partners for ACK1 we found multiple Src family kinases; of these c-Src itself binds best. The SH2 and SH3 domains of Src interact with ACK1 Tyr518 and residues 623–652 respectively. Src targets the ACK1 activation loop Tyr284, a poor autophosphorylation site. We propose that ACK1 fails to undergo significant autophosphorylation on Tyr284in vivo because it is basophilic (whereas Src is acidophilic). Subsequent ACK1 activation downstream of receptors such as EGFR (EGF receptor) (and Src) promotes turnover of ACK1 in vivo, which is blocked by Src inhibitors, and is compromised in the Src-deficient SYF cell line. The results of the present study can explain why ACK1 is responsive to so many external stimuli including RTKs and integrin ligation, since Src kinases are commonly recruited by multiple receptor systems.

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5

Liu, Xia, Xuan Wang, Lifang Li, and Baolin Han. "Research Progress of the Functional Role of ACK1 in Breast Cancer." BioMed Research International 2019 (October 20, 2019): 1–6. http://dx.doi.org/10.1155/2019/1018034.

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ACK1 is a nonreceptor tyrosine kinase with a unique structure, which is tightly related to the biological behavior of tumors. Previous studies have demonstrated that ACK1 was involved with multiple signaling pathways of tumor progression. Its crucial role in tumor cell proliferation, apoptosis, invasion, and metastasis was tightly related to the prognosis and clinicopathology of cancer. ACK1 has a unique way of regulating cellular pathways, different from other nonreceptor tyrosine kinases. As an oncogenic kinase, recent studies have shown that ACK1 plays a critical regulatory role in the initiation and progression of tumors. In this review, we will be summarizing the structural characteristics, activation, and regulation of ACK1 in breast cancer, aiming to deeply understand the functional and mechanistic role of ACK1 and provide novel therapeutic strategies for breast cancer treatment.

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6

Wu, Sijia, Karl D. Bellve, Kevin E. Fogarty, and Haley E. Melikian. "Ack1 is a dopamine transporter endocytic brake that rescues a trafficking-dysregulated ADHD coding variant." Proceedings of the National Academy of Sciences 112, no. 50 (November 30, 2015): 15480–85. http://dx.doi.org/10.1073/pnas.1512957112.

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The dopamine (DA) transporter (DAT) facilitates high-affinity presynaptic DA reuptake that temporally and spatially constrains DA neurotransmission. Aberrant DAT function is implicated in attention-deficit/hyperactivity disorder and autism spectrum disorder. DAT is a major psychostimulant target, and psychostimulant reward strictly requires binding to DAT. DAT function is acutely modulated by dynamic membrane trafficking at the presynaptic terminal and a PKC-sensitive negative endocytic mechanism, or “endocytic brake,” controls DAT plasma membrane stability. However, the molecular basis for the DAT endocytic brake is unknown, and it is unknown whether this braking mechanism is unique to DAT or common to monoamine transporters. Here, we report that the cdc42-activated, nonreceptor tyrosine kinase, Ack1, is a DAT endocytic brake that stabilizes DAT at the plasma membrane and is released in response to PKC activation. Pharmacologic and shRNA-mediated Ack1 silencing enhanced basal DAT internalization and blocked PKC-stimulated DAT internalization, but had no effects on SERT endocytosis. Both cdc42 activation and PKC stimulation converge on Ack1 to control Ack1 activity and DAT endocytic capacity, and Ack1 inactivation is required for stimulated DAT internalization downstream of PKC activation. Moreover, constitutive Ack1 activation is sufficient to rescue the gain-of-function endocytic phenotype exhibited by the ADHD DAT coding variant, R615C. These findings reveal a unique endocytic control switch that is highly specific for DAT. Moreover, the ability to rescue the DAT(R615C) coding variant suggests that manipulating DAT trafficking mechanisms may be a potential therapeutic approach to correct DAT coding variants that exhibit trafficking dysregulation.

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7

Gajiwala, Ketan S., Karen Maegley, RoseAnn Ferre, You-Ai He, and Xiu Yu. "Ack1: Activation and Regulation by Allostery." PLoS ONE 8, no. 1 (January 14, 2013): e53994. http://dx.doi.org/10.1371/journal.pone.0053994.

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8

Furlow, Bryant. "Tyrosine kinase ACK1 promotes prostate tumorigenesis." Lancet Oncology 7, no. 1 (January 2006): 17. http://dx.doi.org/10.1016/s1470-2045(05)70525-8.

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9

del Mar Masdeu, Maria, Beatriz G. Armendáriz, Anna La Torre, Eduardo Soriano, Ferran Burgaya, and Jesús Mariano Ureña. "Identification of novel Ack1-interacting proteins and Ack1 phosphorylated sites in mouse brain by mass spectrometry." Oncotarget 8, no. 60 (September 15, 2017): 101146–57. http://dx.doi.org/10.18632/oncotarget.20929.

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10

Mahajan, Nupam P., Young E. Whang, James L. Mohler, and H. Shelton Earp. "Activated Tyrosine Kinase Ack1 Promotes Prostate Tumorigenesis: Role of Ack1 in Polyubiquitination of Tumor Suppressor Wwox." Cancer Research 65, no. 22 (November 15, 2005): 10514–23. http://dx.doi.org/10.1158/0008-5472.can-05-1127.

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11

Yokoyama, Noriko, Julie Lougheed, and W. Todd Miller. "Phosphorylation of WASP by the Cdc42-associated Kinase ACK1." Journal of Biological Chemistry 280, no. 51 (October 28, 2005): 42219–26. http://dx.doi.org/10.1074/jbc.m506996200.

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12

Yokoyama, Noriko, and W. Todd Miller. "Biochemical Properties of the Cdc42-associated Tyrosine Kinase ACK1." Journal of Biological Chemistry 278, no. 48 (September 22, 2003): 47713–23. http://dx.doi.org/10.1074/jbc.m306716200.

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13

Mahajan, Kiran, and Nupam P. Mahajan. "Shepherding AKT and androgen receptor by Ack1 tyrosine kinase." Journal of Cellular Physiology 224, no. 2 (April 16, 2010): 327–33. http://dx.doi.org/10.1002/jcp.22162.

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14

Mahajan, Kiran, Domenico Coppola, Y. Ann Chen, Weiwei Zhu, Harshani R. Lawrence, Nicholas J. Lawrence, and Nupam P. Mahajan. "Ack1 Tyrosine Kinase Activation Correlates with Pancreatic Cancer Progression." American Journal of Pathology 180, no. 4 (April 2012): 1386–93. http://dx.doi.org/10.1016/j.ajpath.2011.12.028.

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15

Prieto-Echagüe, Victoria, Azad Gucwa, Barbara P. Craddock, Deborah A. Brown, and W. Todd Miller. "Cancer-associated Mutations Activate the Nonreceptor Tyrosine Kinase Ack1." Journal of Biological Chemistry 285, no. 14 (January 28, 2010): 10605–15. http://dx.doi.org/10.1074/jbc.m109.060459.

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16

Nonami, Atsushi, Martin Sattler, Ellen Weisberg, Qingsong Liu, Jianming Zhang, Matthew P. Patricelli, Amanda L. Christie, et al. "Identification of novel therapeutic targets in acute leukemias with NRAS mutations using a pharmacologic approach." Blood 125, no. 20 (May 14, 2015): 3133–43. http://dx.doi.org/10.1182/blood-2014-12-615906.

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Key Points We report a cell-based pharmacologic screening strategy to identify new therapeutic targets in mutant NRAS transformed leukemia cells. The screen and mechanistic analysis identified a previously unknown synergy between germinal center kinase and ACK1/AKT in mutant NRAS transformed cells.

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17

Grøvdal, Lene Melsæther, Lene E. Johannessen, Marianne Skeie Rødland, Inger Helene Madshus, and Espen Stang. "Dysregulation of Ack1 inhibits down-regulation of the EGF receptor." Experimental Cell Research 314, no. 6 (April 2008): 1292–300. http://dx.doi.org/10.1016/j.yexcr.2007.12.017.

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18

Modzelewska, Katarzyna, Laura P. Newman, Radhika Desai, and Patricia J. Keely. "Ack1 Mediates Cdc42-dependent Cell Migration and Signaling to p130Cas." Journal of Biological Chemistry 281, no. 49 (October 12, 2006): 37527–35. http://dx.doi.org/10.1074/jbc.m604342200.

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19

Mahajan, Kiran, Domenico Coppola, Sridevi Challa, Bin Fang, Y. Ann Chen, Weiwei Zhu, Alexis S. Lopez, et al. "Ack1 Mediated AKT/PKB Tyrosine 176 Phosphorylation Regulates Its Activation." PLoS ONE 5, no. 3 (March 19, 2010): e9646. http://dx.doi.org/10.1371/journal.pone.0009646.

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20

Mahajan, K., and N. P. Mahajan. "ACK1/TNK2 tyrosine kinase: An emerging target for cancer therapeutics." AACR Education book 2014, no. 1 (April 4, 2014): 97–102. http://dx.doi.org/10.1158/aacr.edb-14-6109.

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21

Mahajan, Kiran, and Nupam P. Mahajan. "ACK1 tyrosine kinase: Targeted inhibition to block cancer cell proliferation." Cancer Letters 338, no. 2 (September 2013): 185–92. http://dx.doi.org/10.1016/j.canlet.2013.04.004.

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22

Chua, B. T., Y. D. Cheng, and S. C. Tham. "730: ACK1 is a potential target for anti-metastasis therapeutic development." European Journal of Cancer 50 (July 2014): S175. http://dx.doi.org/10.1016/s0959-8049(14)50642-9.

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23

Lawrence, Harshani R., Kiran Mahajan, Yunting Luo, Daniel Zhang, Nathan Tindall, Miles Huseyin, Harsukh Gevariya, et al. "Development of Novel ACK1/TNK2 Inhibitors Using a Fragment-Based Approach." Journal of Medicinal Chemistry 58, no. 6 (March 17, 2015): 2746–63. http://dx.doi.org/10.1021/jm501929n.

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24

Lei, Xiong, Yun-feng Li, Guo-dong Chen, Di-peng Ou, Xiao-xin Qiu, Chao-hui Zuo, and Lian-Yue Yang. "Ack1 overexpression promotes metastasis and indicates poor prognosis of hepatocellular carcinoma." Oncotarget 6, no. 38 (October 20, 2015): 40622–41. http://dx.doi.org/10.18632/oncotarget.5872.

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25

Mahajan, K., and N. P. Mahajan. "ACK1/TNK2 tyrosine kinase: molecular signaling and evolving role in cancers." Oncogene 34, no. 32 (October 27, 2014): 4162–67. http://dx.doi.org/10.1038/onc.2014.350.

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26

van der Horst, E. H., Y. Y. Degenhardt, A. Strelow, A. Slavin, L. Chinn, J. Orf, M. Rong, et al. "Metastatic properties and genomic amplification of the tyrosine kinase gene ACK1." Proceedings of the National Academy of Sciences 102, no. 44 (October 24, 2005): 15901–6. http://dx.doi.org/10.1073/pnas.0508014102.

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27

XIE, BINHUI, QINSHAN ZEN, XIAONONG WANG, XIAO HE, YUANKANG XIE, ZIXIANG ZHANG, and HEPING LI. "ACK1 promotes hepatocellular carcinoma progression via downregulating WWOX and activating AKT signaling." International Journal of Oncology 46, no. 5 (February 27, 2015): 2057–66. http://dx.doi.org/10.3892/ijo.2015.2910.

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28

La Torre, Anna, José Antonio del Rio, Eduardo Soriano, and Jesús Mariano Ureña. "Expression pattern of ACK1 tyrosine kinase during brain development in the mouse." Gene Expression Patterns 6, no. 8 (October 2006): 886–92. http://dx.doi.org/10.1016/j.modgep.2006.02.009.

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29

Xu, Song-Hui, Jin-Zhou Huang, Min Chen, Ming Zeng, Fei-Yan Zou, De Chen, and Guang-Rong Yan. "Amplification of ACK1 promotes gastric tumorigenesis via ECD-dependent p53 ubiquitination degradation." Oncotarget 8, no. 8 (October 20, 2015): 12705–16. http://dx.doi.org/10.18632/oncotarget.6194.

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30

Prieto-Echagüe, Victoria, Azad Gucwa, Deborah A. Brown, and W. Miller. "Regulation of Ack1 localization and activity by the amino-terminal SAM domain." BMC Biochemistry 11, no. 1 (2010): 42. http://dx.doi.org/10.1186/1471-2091-11-42.

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31

Pao-Chun, Lin, Perry M. Chan, Wing Chan, and Ed Manser. "Cytoplasmic ACK1 Interaction with Multiple Receptor Tyrosine Kinases Is Mediated by Grb2." Journal of Biological Chemistry 284, no. 50 (October 8, 2009): 34954–63. http://dx.doi.org/10.1074/jbc.m109.072660.

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32

Mahendrarajah, Nisintha, Marina E. Borisova, Sigrid Reichardt, Maren Godmann, Andreas Sellmer, Siavosh Mahboobi, Andrea Haitel, et al. "HSP90 is necessary for the ACK1-dependent phosphorylation of STAT1 and STAT3." Cellular Signalling 39 (November 2017): 9–17. http://dx.doi.org/10.1016/j.cellsig.2017.07.014.

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33

Han, Woong, Hae-Ik Rhee, Jeong Woo Cho, Maurice S. B. Ku, Pill Soon Song, and Myeong-Hyeon Wang. "Overexpression of Arabidopsis ACK1 alters leaf morphology and retards growth and development." Biochemical and Biophysical Research Communications 330, no. 3 (May 2005): 887–90. http://dx.doi.org/10.1016/j.bbrc.2005.03.056.

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34

Pourbasheer, Eslam, Reza Aalizadeh, Mohammad Reza Ganjali, Parviz Norouzi, and Javad Shadmanesh. "QSAR study of ACK1 inhibitors by genetic algorithm–multiple linear regression (GA–MLR)." Journal of Saudi Chemical Society 18, no. 5 (November 2014): 681–88. http://dx.doi.org/10.1016/j.jscs.2014.01.010.

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35

Kato, Juran, Yoshito Kaziro, and Takaya Satoh. "Activation of the Guanine Nucleotide Exchange Factor Dbl Following ACK1-Dependent Tyrosine Phosphorylation." Biochemical and Biophysical Research Communications 268, no. 1 (February 2000): 141–47. http://dx.doi.org/10.1006/bbrc.2000.2106.

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36

Mahajan, Kiran, Domenico Coppola, Bhupendra Rawal, Y. Ann Chen, Harshani R. Lawrence, Robert W. Engelman, Nicholas J. Lawrence, and Nupam P. Mahajan. "Ack1-mediated Androgen Receptor Phosphorylation Modulates Radiation Resistance in Castration-resistant Prostate Cancer." Journal of Biological Chemistry 287, no. 26 (May 7, 2012): 22112–22. http://dx.doi.org/10.1074/jbc.m112.357384.

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37

Eley, Lorraine, Shabbir H. Moochhala, Roslyn Simms, Friedhelm Hildebrandt, and John A. Sayer. "Nephrocystin-1 interacts directly with Ack1 and is expressed in human collecting duct." Biochemical and Biophysical Research Communications 371, no. 4 (July 2008): 877–82. http://dx.doi.org/10.1016/j.bbrc.2008.05.016.

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38

Yeow-Fong, Lee, Louis Lim, and Ed Manser. "SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1." FEBS Letters 579, no. 22 (August 19, 2005): 5040–48. http://dx.doi.org/10.1016/j.febslet.2005.07.093.

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39

Brandao, Rafael, Mei Qi Kwa, Yossi Yarden, and Cord Brakebusch. "ACK1 is dispensable for development, skin tumor formation, and breast cancer cell proliferation." FEBS Open Bio 11, no. 6 (May 2, 2021): 1579–92. http://dx.doi.org/10.1002/2211-5463.13149.

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40

Kumar, Vikas, Raj Kumar, Shraddha Parate, Sanghwa Yoon, Gihwan Lee, Donghwan Kim, and Keun Woo Lee. "Identification of ACK1 inhibitors as anticancer agents by using computer-aided drug designing." Journal of Molecular Structure 1235 (July 2021): 130200. http://dx.doi.org/10.1016/j.molstruc.2021.130200.

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41

Wu, Sijia. "Rescuing dysfunctional dopamine transporter trafficking: a role for the non-receptor tyrosine kinase, Ack1." Intrinsic Activity 4, Suppl. 2 (August 29, 2016): A18.28. http://dx.doi.org/10.25006/ia.4.s2-a18.28.

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42

Li, Yingming, and Kenneth S. Koeneman. "Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation." Urologic Oncology: Seminars and Original Investigations 26, no. 1 (January 2008): 106–7. http://dx.doi.org/10.1016/j.urolonc.2007.11.019.

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43

Mahajan, N. P., Y. Liu, S. Majumder, M. R. Warren, C. E. Parker, J. L. Mohler, H. S. Earp, and Y. E. Whang. "Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation." Proceedings of the National Academy of Sciences 104, no. 20 (May 9, 2007): 8438–43. http://dx.doi.org/10.1073/pnas.0700420104.

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44

Liu, Y., M. Karaca, Z. Zhang, D. Gioeli, H. S. Earp, and Y. E. Whang. "Dasatinib inhibits site-specific tyrosine phosphorylation of androgen receptor by Ack1 and Src kinases." Oncogene 29, no. 22 (April 12, 2010): 3208–16. http://dx.doi.org/10.1038/onc.2010.103.

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45

Xu, Song-Hui, Jin-Zhou Huang, Man-Li Xu, Guangchuang Yu, Xing-Feng Yin, De Chen, and Guang-Rong Yan. "ACK1 promotes gastric cancer epithelial-mesenchymal transition and metastasis through AKT-POU2F1-ECD signalling." Journal of Pathology 236, no. 2 (March 9, 2015): 175–85. http://dx.doi.org/10.1002/path.4515.

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46

Buchwald, M., K. Pietschmann, P. Brand, A. Günther, N. P. Mahajan, T. Heinzel, and O. H. Krämer. "SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation." Oncogene 32, no. 41 (December 3, 2012): 4913–20. http://dx.doi.org/10.1038/onc.2012.515.

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47

Jin, Meizhong, Jing Wang, Andrew Kleinberg, Mridula Kadalbajoo, Kam W. Siu, Andrew Cooke, Mark A. Bittner, et al. "Discovery of potent, selective and orally bioavailable imidazo[1,5-a]pyrazine derived ACK1 inhibitors." Bioorganic & Medicinal Chemistry Letters 23, no. 4 (February 2013): 979–84. http://dx.doi.org/10.1016/j.bmcl.2012.12.042.

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48

Xiao, Shou-Hua, Ellyn Farrelly, John Anzola, Daniel Crawford, XianYun Jiao, Jinqian Liu, Merrill Ayres, et al. "An ultrasensitive high-throughput electrochemiluminescence immunoassay for the Cdc42-associated protein tyrosine kinase ACK1." Analytical Biochemistry 367, no. 2 (August 2007): 179–89. http://dx.doi.org/10.1016/j.ab.2007.05.007.

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49

Krause, Sue A., Hong Xu, and Joseph V. Gray. "The Synthetic Genetic Network around PKC1 Identifies Novel Modulators and Components of Protein Kinase C Signaling in Saccharomyces cerevisiae." Eukaryotic Cell 7, no. 11 (September 19, 2008): 1880–87. http://dx.doi.org/10.1128/ec.00222-08.

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ABSTRACT Budding yeast Saccharomyces cerevisiae contains one protein kinase C (PKC) isozyme encoded by the essential gene PKC1. Pkc1 is activated by the small GTPase Rho1 and plays a central role in the cell wall integrity (CWI) signaling pathway. This pathway acts primarily to remodel the cell surface throughout the normal life cycle and upon various environmental stresses. The pathway is heavily branched, with multiple nonessential branches feeding into and out of the central essential Rho1-Pkc1 module. In an attempt to identify novel components and modifiers of CWI signaling, we determined the synthetic lethal genetic network around PKC1 by using dominant-negative synthetic genetic array analysis. The resulting mutants are hypersensitive to lowered Pkc1 activity. The corresponding 21 nonessential genes are closely related to CWI function: 14 behave in a chemical-genetic epistasis test as acting in the pathway, and 6 of these genes encode known components. Twelve of the 21 null mutants display elevated CWI reporter activity, consistent with the idea that the pathway is activated by and compensates for loss of the gene products. Four of the 21 mutants display low CWI reporter activity, consistent with the idea that the pathway is compromised in these mutants. One of the latter group of mutants lacks Ack1(Ydl203c), an uncharacterized SEL-1 domain-containing protein that we find modulates pathway activity. Epistasis analysis places Ack1 upstream of Pkc1 in the CWI pathway and dependent on the upstream Rho1 GTP exchange factors Rom2 and Tus1. Overall, the synthetic genetic network around PKC1 directly and efficiently identifies known and novel components of PKC signaling in yeast.

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50

Fagan, Rita R., Patrick J. Kearney, Carolyn G. Sweeney, Dino Luethi, Florianne E. Schoot Uiterkamp, Klaus Schicker, Brian S. Alejandro, Lauren C. O'Connor, Harald H. Sitte, and Haley E. Melikian. "Dopamine transporter trafficking and Rit2 GTPase: Mechanism of action and in vivo impact." Journal of Biological Chemistry 295, no. 16 (March 4, 2020): 5229–44. http://dx.doi.org/10.1074/jbc.ra120.012628.

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Abstract:

Following its evoked release, dopamine (DA) signaling is rapidly terminated by presynaptic reuptake, mediated by the cocaine-sensitive DA transporter (DAT). DAT surface availability is dynamically regulated by endocytic trafficking, and direct protein kinase C (PKC) activation acutely diminishes DAT surface expression by accelerating DAT internalization. Previous cell line studies demonstrated that PKC-stimulated DAT endocytosis requires both Ack1 inactivation, which releases a DAT-specific endocytic brake, and the neuronal GTPase, Rit2, which binds DAT. However, it is unknown whether Rit2 is required for PKC-stimulated DAT endocytosis in DAergic terminals or whether there are region- and/or sex-dependent differences in PKC-stimulated DAT trafficking. Moreover, the mechanisms by which Rit2 controls PKC-stimulated DAT endocytosis are unknown. Here, we directly examined these important questions. Ex vivo studies revealed that PKC activation acutely decreased DAT surface expression selectively in ventral, but not dorsal, striatum. AAV-mediated, conditional Rit2 knockdown in DAergic neurons impacted baseline DAT surface:intracellular distribution in DAergic terminals from female ventral, but not dorsal, striatum. Further, Rit2 was required for PKC-stimulated DAT internalization in both male and female ventral striatum. FRET and surface pulldown studies in cell lines revealed that PKC activation drives DAT-Rit2 surface dissociation and that the DAT N terminus is required for both PKC-mediated DAT-Rit2 dissociation and DAT internalization. Finally, we found that Rit2 and Ack1 independently converge on DAT to facilitate PKC-stimulated DAT endocytosis. Together, our data provide greater insight into mechanisms that mediate PKC-regulated DAT internalization and reveal unexpected region-specific differences in PKC-stimulated DAT trafficking in bona fide DAergic terminals.

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