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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 (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

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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 (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 indic

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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 i

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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 (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

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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 init

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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 (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 th

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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 (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 (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 (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 (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 (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 (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 (2010): 327–33. http://dx.doi.org/10.1002/jcp.22162.

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14

Mahajan, Kiran, Domenico Coppola, Y. Ann Chen, et al. "Ack1 Tyrosine Kinase Activation Correlates with Pancreatic Cancer Progression." American Journal of Pathology 180, no. 4 (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 (2010): 10605–15. http://dx.doi.org/10.1074/jbc.m109.060459.

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16

Nonami, Atsushi, Martin Sattler, Ellen Weisberg, et al. "Identification of novel therapeutic targets in acute leukemias with NRAS mutations using a pharmacologic approach." Blood 125, no. 20 (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 (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 (2006): 37527–35. http://dx.doi.org/10.1074/jbc.m604342200.

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19

Mahajan, Kiran, Domenico Coppola, Sridevi Challa, et al. "Ack1 Mediated AKT/PKB Tyrosine 176 Phosphorylation Regulates Its Activation." PLoS ONE 5, no. 3 (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 (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 (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, et al. "Development of Novel ACK1/TNK2 Inhibitors Using a Fragment-Based Approach." Journal of Medicinal Chemistry 58, no. 6 (2015): 2746–63. http://dx.doi.org/10.1021/jm501929n.

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24

Lei, Xiong, Yun-feng Li, Guo-dong Chen, et al. "Ack1 overexpression promotes metastasis and indicates poor prognosis of hepatocellular carcinoma." Oncotarget 6, no. 38 (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 (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, et al. "Metastatic properties and genomic amplification of the tyrosine kinase gene ACK1." Proceedings of the National Academy of Sciences 102, no. 44 (2005): 15901–6. http://dx.doi.org/10.1073/pnas.0508014102.

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27

XIE, BINHUI, QINSHAN ZEN, XIAONONG WANG, et al. "ACK1 promotes hepatocellular carcinoma progression via downregulating WWOX and activating AKT signaling." International Journal of Oncology 46, no. 5 (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 (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, et al. "Amplification of ACK1 promotes gastric tumorigenesis via ECD-dependent p53 ubiquitination degradation." Oncotarget 8, no. 8 (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 (2009): 34954–63. http://dx.doi.org/10.1074/jbc.m109.072660.

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32

Mahendrarajah, Nisintha, Marina E. Borisova, Sigrid Reichardt, 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 (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 (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 (2000): 141–47. http://dx.doi.org/10.1006/bbrc.2000.2106.

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36

Mahajan, Kiran, Domenico Coppola, Bhupendra Rawal, et al. "Ack1-mediated Androgen Receptor Phosphorylation Modulates Radiation Resistance in Castration-resistant Prostate Cancer." Journal of Biological Chemistry 287, no. 26 (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 (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 (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 (2021): 1579–92. http://dx.doi.org/10.1002/2211-5463.13149.

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40

Kumar, Vikas, Raj Kumar, Shraddha Parate, et al. "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 (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 (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, et al. "Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation." Proceedings of the National Academy of Sciences 104, no. 20 (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 (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, et al. "ACK1 promotes gastric cancer epithelial-mesenchymal transition and metastasis through AKT-POU2F1-ECD signalling." Journal of Pathology 236, no. 2 (2015): 175–85. http://dx.doi.org/10.1002/path.4515.

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46

Buchwald, M., K. Pietschmann, P. Brand, et al. "SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation." Oncogene 32, no. 41 (2012): 4913–20. http://dx.doi.org/10.1038/onc.2012.515.

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47

Jin, Meizhong, Jing Wang, Andrew Kleinberg, et al. "Discovery of potent, selective and orally bioavailable imidazo[1,5-a]pyrazine derived ACK1 inhibitors." Bioorganic & Medicinal Chemistry Letters 23, no. 4 (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, et al. "An ultrasensitive high-throughput electrochemiluminescence immunoassay for the Cdc42-associated protein tyrosine kinase ACK1." Analytical Biochemistry 367, no. 2 (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 (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

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50

Fagan, Rita R., Patrick J. Kearney, Carolyn G. Sweeney, et al. "Dopamine transporter trafficking and Rit2 GTPase: Mechanism of action and in vivo impact." Journal of Biological Chemistry 295, no. 16 (2020): 5229–44. http://dx.doi.org/10.1074/jbc.ra120.012628.

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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

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