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Gotowe bibliografie tematyczne / PACSIN2

Gotowa bibliografia na temat „PACSIN2”

Autor: Grafiati

Data publikacji: 1 kwietnia 2023

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Artykuły w czasopismach na temat "PACSIN2":

1

Zudeh, Giulia, Raffaella Franca, Marianna Lucafò, Erik J. Bonten, Matteo Bramuzzo, Riccardo Sgarra, Cristina Lagatolla i in. "PACSIN2as a modulator of autophagy and mercaptopurine cytotoxicity: mechanisms in lymphoid and intestinal cells". Life Science Alliance 6, nr 3 (3.01.2023): e202201610. http://dx.doi.org/10.26508/lsa.202201610.

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PACSIN2 variants are associated with gastrointestinal effects of thiopurines and thiopurine methyltransferase activity through an uncharacterized mechanism that is postulated to involve autophagy. This study aims to clarify the role of PACSIN2 in autophagy and in thiopurine cytotoxicity in leukemic and intestinal models. Higher autophagy and lower PACSIN2 levels were observed in inflamed compared with non-inflamed colon biopsies of inflammatory bowel disease pediatric patients at diagnosis. PACSIN2 was identified as an inhibitor of autophagy, putatively through inhibition of autophagosome formation by a protein–protein interaction with LC3-II, mediated by a LIR motif. Moreover, PACSIN2 resulted a modulator of mercaptopurine-induced cytotoxicity in intestinal cells, suggesting that PACSIN2-regulated autophagy levels might influence thiopurine sensitivity. However, PACSIN2 modulates cellular thiopurine methyltransferase activity via mechanisms distinct from its modulation of autophagy.

2

Nishimura, Tamako, i Shiro Suetsugu. "Super-resolution analysis of PACSIN2 and EHD2 at caveolae". PLOS ONE 17, nr 7 (14.07.2022): e0271003. http://dx.doi.org/10.1371/journal.pone.0271003.

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Caveolae are plasma membrane invaginations that play important roles in both endocytosis and membrane tension buffering. Typical caveolae have invaginated structures with a high-density caveolin assembly. Membrane sculpting proteins, including PACSIN2 and EHD2, are involved in caveolar biogenesis. PACSIN2 is an F-BAR domain-containing protein with a membrane sculpting ability that is essential for caveolar shaping. EHD2 is also localized at caveolae and involved in their stability. However, the spatial relationship between PACSIN2, EHD2, and caveolin has not yet been investigated. We observed the single-molecule localizations of PACSIN2 and EHD2 relative to caveolin-1 in three-dimensional space. The single-molecule localizations were grouped by their proximity localizations into the geometric structures of blobs. In caveolin-1 blobs, PACSIN2, EHD2, and caveolin-1 had overlapped spatial localizations. Interestingly, the mean centroid of the PACSIN2 F-BAR domain at the caveolin-1 blobs was closer to the plasma membrane than those of EHD2 and caveolin-1, suggesting that PACSIN2 is involved in connecting caveolae to the plasma membrane. Most of the blobs with volumes typical of caveolae had PACSIN2 and EHD2, in contrast to those with smaller volumes. Therefore, PACSIN2 and EHD2 are apparently localized at typically sized caveolae.

3

Gusmira, Aini, Kazuhiro Takemura, Shin Yong Lee, Takehiko Inaba, Kyoko Hanawa-Suetsugu, Kayoko Oono-Yakura, Kazuma Yasuhara, Akio Kitao i Shiro Suetsugu. "Regulation of caveolae through cholesterol-depletion-dependent tubulation mediated by PACSIN2". Journal of Cell Science 133, nr 19 (2.09.2020): jcs246785. http://dx.doi.org/10.1242/jcs.246785.

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ABSTRACTThe membrane-shaping ability of PACSIN2 (also known as syndapin II), which is mediated by its F-BAR domain, has been shown to be essential for caveolar morphogenesis, presumably through the shaping of the caveolar neck. Caveolar membranes contain abundant cholesterol. However, the role of cholesterol in PACSIN2-mediated membrane deformation remains unclear. Here, we show that the binding of PACSIN2 to the membrane can be negatively regulated by cholesterol. We prepared reconstituted membranes based on the lipid composition of caveolae. The reconstituted membrane with cholesterol had a weaker affinity for the F-BAR domain of PACSIN2 than a membrane without cholesterol. Consistent with this, upon depletion of cholesterol from the plasma membrane, PACSIN2 localized at tubules that had caveolin-1 at their tips, suggesting that cholesterol inhibits membrane tubulation mediated by PACSIN2. The tubules induced by PACSIN2 could be representative of an intermediate of caveolae endocytosis. Consistent with this, the removal of caveolae from the plasma membrane upon cholesterol depletion was diminished in the PACSIN2-deficient cells. These data suggest that PACSIN2-mediated caveolae internalization is dependent on the amount of cholesterol, providing a mechanism for cholesterol-dependent regulation of caveolae.This article has an associated First Person interview with the first author of the paper.

4

Popov, Sergei, Elena Popova, Michio Inoue, Yuanfei Wu i Heinrich Göttlinger. "HIV-1 gag recruits PACSIN2 to promote virus spreading". Proceedings of the National Academy of Sciences 115, nr 27 (11.06.2018): 7093–98. http://dx.doi.org/10.1073/pnas.1801849115.

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The p2b domain of Rous sarcoma virus (RSV) Gag and the p6 domain of HIV-1 Gag contain late assembly (L) domains that engage the ESCRT membrane fission machinery and are essential for virus release. We now show that the PPXY-type RSV L domain specifically recruits the BAR domain protein PACSIN2 into virus-like particles (VLP), in addition to the NEDD4-like ubiquitin ligase ITCH and ESCRT pathway components such as TSG101. PACSIN2, which has been implicated in the remodeling of cellular membranes and the actin cytoskeleton, is also recruited by HIV-1 p6 independent of its ability to engage the ESCRT factors TSG101 or ALIX. Moreover, PACSIN2 is robustly recruited by NEDD4-2s, a NEDD4-like ubiquitin ligase capable of rescuing HIV-1 budding defects. The NEDD4-2s–induced incorporation of PACSIN2 into VLP correlated with the formation of Gag-ubiquitin conjugates, indicating that PACSIN2 binds ubiquitin. Although PACSIN2 was not required for a single cycle of HIV-1 replication after infection with cell-free virus, HIV-1 spreading was nevertheless severely impaired in T cell lines and primary human peripheral blood mononuclear cells depleted of PACSIN2. HIV-1 spreading could be restored by reintroduction of wild-type PACSIN2, but not of a SH3 domain mutant unable to interact with the actin polymerization regulators WASP and N-WASP. Overall, our observations indicate that PACSIN2 promotes the cell-to-cell spreading of HIV-1 by connecting Gag to the actin cytoskeleton.

5

Giannini, Silvia, Markus Bender, Fred G. Pluthero, Hilary Christensen, Richard Leung, Richard W. Lo, Jan Kormann, Markus Plomann, Walter H. A. Kahr i Hervé Falet. "Dynamin 2 (DNM2) and PACSIN2 Regulate Megakaryocyte Demarcation Membrane System Formation and Platelet Production in Concert". Blood 126, nr 23 (3.12.2015): 419. http://dx.doi.org/10.1182/blood.v126.23.419.419.

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Abstract Blood platelets are produced in the bone marrow by megakaryocytes (MKs) in a process that requires extensive intracellular membrane rearrangements. These include the formation of the demarcation membrane system (DMS), the surface-connected membrane extension that invaginates into the cell body and further develops to provide membranes for future platelets. The precise molecular mechanisms responsible for these unique membrane rearrangements remain poorly understood. We have recently shown that Dnm2fl/fl Pf4-Cre mice specifically lacking the large GTPase dynamin 2 (DNM2) in MKs develop severe macrothrombocytopenia due to impaired receptor-mediated endocytosis (RME) (Bender, Giannini et al. Blood. 2015;125(6):1014-1024). Specifically, Dnm2fl/fl Pf4-Cre MKs accumulate arrested endocytic clathrin-coated vesicles that obstruct DMS formation. The actin nucleating factor Arp2/3 complex and polymerized actin clustered with clathrin at sites of impaired RME in Dnm2fl/fl Pf4-Cre MKs. We hypothesized that a DNM2 partner recruits actin-regulatory proteins at sites of RME and investigated the contribution of the F-BAR protein PACSIN2, an internal component of the initiating DMS (Jurak Begonja, Pluthero et al. Blood. 2015;126(1):80-88), in DMS formation and platelet production, as PACSIN2 interacts with DNM2 and actin-regulatory proteins such as N-WASP and filamin A (FlnA). Pacsin2-/- mice developed mild thrombocytopenia with slightly enlarged and shallow platelets. The DMS appeared less well defined and platelet territories were not readily visualized in Pacsin2-/- MKs. Pacsin2-/- Dnm2fl/fl Pf4-Cre mice lacking both PACSIN2 and DNM2 in MKs were further generated to determine the contribution of PACSIN2 in clathrin and actin clustering in Dnm2fl/fl Pf4-Cre MKs. Strikingly, PACSIN2 genetic deletion significantly improved the severe thrombocytopenia of Dnm2fl/fl Pf4-Cre mice. Specifically, PACSIN2 deletion abrogated the accumulation of clathrin and actin clusters, thereby unclogging DMS formation, which appeared as elongated maze-like membrane tubules in Pacsin2-/- Dnm2fl/fl Pf4-Cre MKs. Our results show that DNM2 terminates PACSIN2-dependent actin polymerization that accompanies RME, thereby allowing membrane rearrangements required for DMS formation. Disclosures No relevant conflicts of interest to declare.

6

Jönsson, Terese, Fred G. Pluthero, Antonija Jurak Begonja, Jan Kormann, Mélanie Demers, Denisa D. Wagner, Markus Plomann, John H. Hartwig, Walter H. Kahr i Hervé Falet. "The F-BAR Protein PACSIN2 Regulates Platelet Intracellular Membrane Architecture and in Vivo Hemostatic Functions". Blood 124, nr 21 (6.12.2014): 4154. http://dx.doi.org/10.1182/blood.v124.21.4154.4154.

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Abstract Proteins of the Bin-amphiphysin-Rvs (BAR) and Fes-CIP4 homology BAR (F-BAR) families bind and deform membranes, promoting in cells tubular invaginations reminiscent of the platelet open canalicular system (OCS) and megakaryocyte (MK) demarcation membrane system (DMS). Here we investigated the role of the F-BAR protein PACSIN2 in platelets and MKs. Spinning disk laser fluorescence confocal microscopy showed that PACSIN2 co-localized with the von Willebrand factor receptor subunit GPIbα at the openings of the OCS in platelets. Endogenous and over-expressed PACSIN2 associated with anastomosing tubular structures reminiscent of the pre-DMS in mouse bone marrow MKs. Pacsin2-null mice had mild thrombocytopenia and polycythemia, MK hyperplasia and splenomegaly. Pacsin2-null mice had a bleeding disorder, as evidenced by significantly prolonged tail bleeding and delayed in vivo thrombus formation following FeCl3 vascular injury, which was normalized by injection of WT platelets. However, Pacsin2-null platelets expressed P-selectin and activated the integrin αIIbβ3 normally in response to stimulation with thrombin and the GPVI-specific collagen-related peptide. In contrast, Pacsin2-null platelets had abnormal flattened morphology, with more and narrower OCS channels on their surface, compared to WT platelets. Together, the data indicate that the F-BAR protein PACSIN2 orchestrates the intracellular membrane architecture of platelets, thereby regulating their in vivo hemostatic functions. Disclosures No relevant conflicts of interest to declare.

7

Postema, Meagan M., Nathan E. Grega-Larson, Leslie M. Meenderink i Matthew J. Tyska. "PACSIN2-dependent apical endocytosis regulates the morphology of epithelial microvilli". Molecular Biology of the Cell 30, nr 19 (1.09.2019): 2515–26. http://dx.doi.org/10.1091/mbc.e19-06-0352.

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Apical microvilli are critical for the homeostasis of transporting epithelia, yet mechanisms that control the assembly and morphology of these protrusions remain poorly understood. Previous studies in intestinal epithelial cell lines suggested a role for the F-BAR domain protein PACSIN2 in normal microvillar assembly. Here we report the phenotype of PACSIN2 KO mice and provide evidence that through its role in promoting apical endocytosis, this molecule plays a role in controlling microvillar morphology. PACSIN2 KO enterocytes exhibit reduced numbers of microvilli and defects in the microvillar ultrastructure, with membranes lifting away from rootlets of core bundles. Dynamin2, a PACSIN2 binding partner, and other endocytic factors were also lost from their normal localization near microvillar rootlets. To determine whether loss of endocytic machinery could explain defects in microvillar morphology, we examined the impact of PACSIN2 KD and endocytosis inhibition on live intestinal epithelial cells. These assays revealed that when endocytic vesicle scission fails, tubules are pulled into the cytoplasm and this, in turn, leads to a membrane-lifting phenomenon reminiscent of that observed at PACSIN2 KO brush borders. These findings lead to a new model where inward forces generated by endocytic machinery on the plasma membrane control the membrane wrapping of cell surface protrusions.

8

Begonja, Antonija Jurak, Fred G. Pluthero, Worawit Suphamungmee, Silvia Giannini, Hilary Christensen, Richard Leung, Richard W. Lo i in. "FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets". Blood 126, nr 1 (2.07.2015): 80–88. http://dx.doi.org/10.1182/blood-2014-07-587600.

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Key PointsThe F-BAR protein PACSIN2 associates with the initiating demarcation membrane system in megakaryocytes. FlnA binding to the PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes, platelets, and in vitro.

9

Sanderlin, Allen G., Cassandra Vondrak, Arianna J. Scricco, Indro Fedrigo, Vida Ahyong i Rebecca L. Lamason. "RNAi screen reveals a role for PACSIN2 and caveolins during bacterial cell-to-cell spread". Molecular Biology of the Cell 30, nr 17 (sierpień 2019): 2124–33. http://dx.doi.org/10.1091/mbc.e19-04-0197.

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Listeria monocytogenes is a human bacterial pathogen that disseminates through host tissues using a process called cell-to-cell spread. This critical yet understudied virulence strategy resembles a vesicular form of intercellular trafficking that allows L. monocytogenes to move between host cells without escaping the cell. Interestingly, eukaryotic cells can also directly exchange cellular components via intercellular communication pathways (e.g., trans-endocytosis) using cell–cell adhesion, membrane trafficking, and membrane remodeling proteins. Therefore, we hypothesized that L. monocytogenes would hijack these types of host proteins during spread. Using a focused RNA interference screen, we identified 22 host genes that are important for L. monocytogenes spread. We then found that caveolins (CAV1 and CAV2) and the membrane sculpting F-BAR protein PACSIN2 promote L. monocytogenes protrusion engulfment during spread, and that PACSIN2 specifically localizes to protrusions. Overall, our study demonstrates that host intercellular communication pathways may be coopted during bacterial spread and that specific trafficking and membrane remodeling proteins promote bacterial protrusion resolution.

10

Chitu, Violeta, i E. Richard Stanley. "PACSIN2: a BAR-rier forming the megakaryocyte DMS". Blood 126, nr 1 (2.07.2015): 5–6. http://dx.doi.org/10.1182/blood-2015-04-639450.

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Więcej źródeł

Rozprawy doktorskie na temat "PACSIN2":

1

COUSIN, HELENE. "Analyse fonctionnelle des proteines adam13 et pacsin2 au cours du developpement de xenopus laevis". Paris 6, 2000. http://www.theses.fr/2000PA066120.

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Les adam sont des glycoproteines transmembranaires possedant a disintegrin and a metalloprotease domain, impliquees dans de nombreux phenomenes cellulaires comme la signalisation ou la migration. Adam13 est un membre de cette famille exprime, chez le xenope, dans les cellules de la crete neurale cephalique (cnc). Nous montrons qu'adam13 est une metalloprotease fonctionnelle qui peut s'autodegrader et remodeler les matrices extracellulaires. La sur-expression de la forme sauvage d'adam13 desorganise la cnc en migration in vivo et perturbe la migration des cellules mesodermiques in vitro. La sur-expression d'adam13 confere aux cellules xtc la capacite de remodeler un substrat de fibronectine. L'expression du mutant catalytiquement inactif e/a dans les embryons ou dans les cellules en culture ne provoque aucun de ces phenomenes, ce qui montre l'importance du domaine metalloprotease dans la fonction d'adam13. Enfin, le mutant dominant negatif e/a est capable d'inhiber la migration des cellules de la cnc in vivo. D'autre part, nous avons recherche des proteines ayant une affinite pour le domaine cytoplasmique. Nous avons mis au point un crible qui nous a permis d'identifier trois proteines capable d'interagir avec le domaine cytoplasmique via leur domaine sh3 : animal4, src1 et pacsin2. Nous avons donc focalise notre etude sur la pacsin2 de xenope. La proteine colocalise avec adam13 dans les cellules de la cnc dans les embryons et dans certaines structures membranaires et vesiculaires dans les cellules xtc. In vivo, la pacsin2 inhibe les phenotypes provoques par la sur-expression d'adam13. La sur-expression de la pacsin2 provoque des phenotypes similaires a ceux provoques par e/a. En revanche, le mutant de pacsin2 delete de son domaine sh3 provoque des phenotypes similaires a ceux provoques par la sur-expression d'adam13. Ces resultats suggerent que la pacsin2 regule la fonction d'adam13 in vivo en perturbant soit son etat de phosphorylation soit sa conformation.

2

Halbach, Arndt. "Proteinbiochemische Charakterisierung von PACSIN1 und seines Bindungspartners PAST2". [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=970525435.

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Modregger, Jan Dieter. "PACSIN und seine SH3-Bindungspartner Wechselwirkungen und Funktionen /". [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962003832.

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Ritter, Brigitte. "Isolierung neuer PACSIN-Isoformen und funktionale Charakterisierung der Protein-Familie". [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962715360.

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5

Gottfried, Russell. "PACSIM : using simulation in designing a communications satellite". Thesis, Monterey, California. Naval Postgraduate School, 1992. http://hdl.handle.net/10945/23746.

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Sikora, Romain. "Recyclage membranaire : rôle de la protéine MICAL-L1 et de son partenaire PACSINE3". Thesis, Sorbonne Paris Cité, 2015. http://www.theses.fr/2015USPCB179/document.

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Le recyclage de récepteurs et de lipides vers la membrane plasmique, est un processus finement régulé, essentiel pour l’homéostasie de la membrane plasmique et pour la migration cellulaire. Il requière l’intervention des petites GTPases de la famille Rabs et leurs effecteurs. La protéine MICAL-L1, effecteur de plusieurs Rabs, comme Rab 8, 11, 13 et 35, a été impliquée dans le recyclage vers la membrane plasmique. Dans cette étude, nous avons identifié une nouvelle interaction entre MICAL-L1 et la PACSINE3, une protéine à domaine F-BAR capable de façonner les membranes intracellulaires et qui contribue à la génération d’endosomes de recyclage tubulaires. MICAL-L1 est nécessaire pour la localisation de la PACSINE3 au niveau des membranes des endosomes. La perturbation du complexe MICAL-L1/PACSINE3 affecte le recyclage du récepteur de la transferrine (TfR) vers la membrane plasmique. Le complexe MICAL-L1/PACSINE3 est associé à des longs tubules membranaires contenant la transferrine comme cargo. La dynamique de ségrégation et de détachement des cargos Tf à partir des tubules contenant MICAL-L1 et PACSINE3, suggère que ce complexe contrôle le tri/adressage des endosomes de recyclage vers la membrane plasmique. Notre travail révèle un nouveau mécanisme de régulation de la voie de recyclage vers la surface cellulaire
The recycling to the plasma membrane of receptors and lipids is tightly regulated and is essential for PM homeostasis, adhesion and cell migration. It requires small GTPase Rab proteins and their effectors. The MICAL-L1 protein, an effector of several Rabs including Rab 8, 11, 13 and 35, has been shown to play an important role in the recycling. Here, we report a novel interaction between MICAL-L1 and the BAR domain containing protein PACSIN3/Syndapin3 that contributes to generate tubular recycling endosomes. MICAL-L1 is required for the localization of PACSIN3 to endosomal membranes. Importantly, disruption of MICAL-L1/PACSIN3 interaction promotes the transferrin receptor (TfR) delivery back to the plasma membrane. The MICAL-L1/PACSIN3 complex accumulates in elongated tubules that contain transferrin carriers. The dynamic of transferrin positive endosomes segregation from MICAL-L1/PACSIN3 tubules suggests that MICAL-L1/PACSIN3 complex controls TfR recycling endosomes delivery to the plasma membrane. Our data provide novel mechanistic insights on the dynamical regulation of the plasma membrane recycling pathway

7

Garcia-Elias, Heras Anna. "Molecular determinants of TRPV4 channel regulation". Doctoral thesis, Universitat Pompeu Fabra, 2011. http://hdl.handle.net/10803/53592.

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TRPV4 is a non-selective cation channel with a wide expression and multiple cellular and systemic functions. Described initially as an osmosensor, it can also be activated by temperature and cell swelling. Due to this variety of activating stimuli it may have a promiscuous gating behavior which is mostly unknown. This Thesis research aims to get in-depth in the understanding of the molecular determinants of TRPV4 regulation. I provide evidences that the inositol trisphosphate receptor and its modulatory function on TRPV4 relies on its binding to the C-terminal tail of TRPV4. I discuss the role of the channels’ N-terminal tail in osmotransduction and show how a mutation that results in a channel with an impaired response to osmotic environments is associated to a pathophysiological condition such as hyponatremia. I also highlight the importance of this N-terminal tail and the binding to the regulatory protein PACSIN3 for the global conformation of the channel.
El TRPV4 és un canal catiònic no selectiu d’expressió generalitzada i funcions diverses. Tot i que inicialment es va descriure com un osmosensor sistèmic, avui sabem que també es pot activar per temperatura o per augments del volum cel•lular. Degut a la diversitat d’estímuls, el canal presenta diferents vies d’activació la major part de les quals són desconegudes. Aquesta Tesi pretén estudiar en detall els mecanismes moleculars que regulen l’activitat del canal. Aportem evidències del lloc d’unió a la cua C-terminal del receptor d’inositol trifosfat així com la seva modulació sobre l’activitat del TRPV4. També discutim el rol de la cua N-terminal en la osmotransducció i presentem una mutació, generadora d’un canal amb una resposta anòmala a estímuls hipotònics, que està associada a una condició fisiopatològica com la hiponatremia. També destaquem la importància de la cua N-terminal i de la unió de la proteïna reguladora PACSIN3 en la conformació global del canal.

8

Desrochers, Guillaume. "Comparaison de l’ubiquitylation de différentes protéines à domaine SH3 impliquées dans l’endocytose suite à leur interaction avec la ligase de l’ubiquitine Itch". Thèse, 2010. http://hdl.handle.net/1866/4314.

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Itch est la seule ligase de l'ubiquitine de type C2-WW-HECT capable d'interagir avec les protéines à domaine SH3. Ce domaine est particulièrement représenté parmi les protéines régulatrices de l'endocytose. Les travaux présentés ici visaient à examiner la capacité d'Itch à interagir avec plusieurs protéines endocytiques. Nous avons utilisé la technique du BRET (Bioluminescence Resonance Energy Transfer) pour examiner quelques protéines candidates. Nous avons ensuite confirmé les résultats obtenus par BRET avec des tests d'interaction in vitro, puis déterminé la capacité d'Itch à ubiquityler les protéines liées via leurs domaines SH3. Nous avons ainsi découvert deux nouveaux partenaires d'interaction et substrats d'Itch parmi les protéines endocytiques, amphyphisine et pacsine. De plus, Itch interagit avec les domaines SH3 isolés d'intersectine, mais pas avec la protéine complète, suggérant que cette dernière n'est pas un substrat d'Itch. Itch est donc bien positionnée pour exercer un rôle régulateur de l'endocytose en ubiquitylant ses substrats.
Itch is the only C2-WW-HECT type ubiquitin ligase that can bind SH3 domain proteins. This domain is particularly frequent in accessory endocytic proteins. We have used Bioluminescent Resonance Energy Transfer to examine a few candidate endocytic proteins, in addition to the already known substrate of Itch, endophilin. We then used standard in vitro techniques to confirm these interactions, and tested Itch capacity to ubiquitylate these putative substrate proteins. We thus discovered two new substrates of Itch, amphiphysin and pacsin. We also determined that although Itch interacts with the isolated SH3 domains of intersectin, it does not recognize the full length protein, thus rulling out Intersectin as a substrate of Itch. Itch is thus a putatively important regulator of endocytosis, through its capacity to recognize and ubiquitylate several SH3-domain proteins.

9

Halbach, Arndt [Verfasser]. "Proteinbiochemische Charakterisierung von PACSIN1 und seines Bindungspartners PAST2 / vorgelegt von Arndt Halbach". 2003. http://d-nb.info/970525435/34.

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Modregger, Jan Dieter [Verfasser]. "PACSIN und seine SH3-Bindungspartner : Wechselwirkungen und Funktionen / vorgelegt von Jan Dieter Modregger". 2001. http://d-nb.info/962003832/34.

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Książki na temat "PACSIN2":

1

Rudolf, Pacsika, i Müllner András, red. Prerock'n'roll: Megjelent Pacsika Rudolf kiállítása alkalmából : Ssentendrei Képtár. [Hungary]: PMMI, 2006.

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2

Gottfried, Russell. PACSIM: Using simulation in designing a communications satellite. Monterey, Calif: Naval Postgraduate School, 1992.

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3

Gottfried, Russell. PACISM [i.e. PACSIM]: A design aid for the development of the Petite Amateur Navy Satellite. Monterey, Calif: Naval Postgraduate School, 1992.

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Części książek na temat "PACSIN2":

1

Cornelis, Eric, i Philippe L. Toint. "PACSIM: A New Dynamic Behavioural Model for Multimodal Traffic Assignment". W Operations Research and Decision Aid Methodologies in Traffic and Transportation Management, 28–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03514-6_2.

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"The PACSIN Proteins and Their Role in Membrane Trafficking". W The Pombe Cdc15 Homology Proteins, 51–60. CRC Press, 2009. http://dx.doi.org/10.1201/9781498712798-10.

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Dumitrache, I., M. Dumitru, C. Vasiliu i C. Opricg. "PACSID - A SOFTWARE PACKAGE FOR DYNAMIC SYSTEMS MODELLING, DESIGN AND SIMULATION". W Applications, 124–28. De Gruyter, 1985. http://dx.doi.org/10.1515/9783112472569-022.

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