CIN85 Associates with Multiple Effectors Controlling Intracellular Trafficking of Epidermal Growth Factor Receptors

Kaczyńska, Katarzyna; Husnjak, Koraljka; Höller, Daniela; Kowanetz, Marcin; Soubeyran, Philippe; Hirsch, Dianne S.; Schmidt, Mirko H. H.; Pavelić, Krešimir; Camilli, Pietro De; Randazzo, Paul A.; Đikić, Ivan

doi:10.1091/mbc.e03-09-0683

Cited by 121 publications

(139 citation statements)

References 65 publications

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“…The specific functions of ARAPs are largely unknown, although they appear to have roles in post-endocytic transport [52], cytoskeletal reorganization in response to growth factors [35], and focal adhesion dynamics [50]. Each of the ARAPs also contains a Ras-association (RA) domain, predicted to serve as a binding site for Ras or for closely related GTPases such as Rap [53].…”

Section: Arapsmentioning

confidence: 99%

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Myers

Casanova

2008

Trends in Cell Biology

167

139

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Small GTPases of the Arf family are best known for their role in vesicular transport, wherein they nucleate the assembly of coat proteins at sites of carrier vesicle formation. However, accumulating evidence indicates that the Arfs are also important regulators of actin cytoskeleton dynamics and are involved in a variety of actin-based processes, including cell adhesion, migration and neurite outgrowth. The mechanisms of this regulation are remarkably diverse, ranging from the integration of vesicular transport with cytoskeleton assembly to the direct regulation of Rho-family GTPase function. Here, we review recent progress in our understanding of how Arfs and their interacting proteins function to integrate membrane and cytoskeletal dynamics.

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Section: Arapsmentioning

confidence: 99%

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Myers

Casanova

2008

Trends in Cell Biology

167

139

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“…In addition, Arf1 also mediates paxillin recruitment to focal adhesions (Norman et al, 1998). We have found that CIN85, a multidomain adaptor protein involved in Cbl-mediated down-regulation of EGFR, interacts with ASAP1, and overexpression of ASAP1 increases the recycling of EGFR in CHO cells (Kowanetz et al, 2004). More recently, CIN85 has been reported to colocalize with ASAP1 in invadopodia, and the complex of ASAP1 and CIN85 has been proposed to positively regulate the invasive phenotype of breast cancer cells (Nam et al, 2007).…”

mentioning

confidence: 94%

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

Self Cite

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ADP-ribosylation factors (Arfs) and Arf GTPase-activating proteins (GAPs) are key regulators of membrane trafficking and the actin cytoskeleton. The Arf GAP ASAP1 contains an N-terminal BAR domain, which can induce membrane tubulation. Here, we report that the BAR domain of ASAP1 can also function as a protein binding site. Two-hybrid screening identified FIP3, which is a putative Arf6-and Rab11-effector, as a candidate ASAP1 BAR domain-binding protein. Both coimmunoprecipitation and in vitro pulldown assays confirmed that ASAP1 directly binds to FIP3 through its BAR domain. ASAP1 formed a ternary complex with Rab11 through FIP3. FIP3 binding to the BAR domain stimulated ASAP1 GAP activity against Arf1, but not Arf6. ASAP1 colocalized with FIP3 in the pericentrosomal endocytic recycling compartment. Depletion of ASAP1 or FIP3 by small interfering RNA changed the localization of transferrin receptor, which is a marker of the recycling endosome, in HeLa cells. The depletion also altered the trafficking of endocytosed transferrin. These results support the conclusion that ASAP1, like FIP3, functions as a component of the endocytic recycling compartment. INTRODUCTIONArf family GTP-binding proteins and their GTPase-activating proteins (Arf GAPs) play crucial roles for membrane traffic and actin remodeling (D'Souza-Schorey and Chavrier, 2006;Gillingham and Munro, 2007). Arf GAPs share the same catalytic domain, the Arf GAP domain, which is responsible for GTP hydrolysis. In humans, 31 genes encoding proteins with Arf GAP domains have been found. They are classified into several subfamilies based on their domain structures Inoue and Randazzo, 2007). Three subfamilies, ArfGAPs, SMAPs, and GITs, have an Arf GAP domain at the N-terminus of the molecules. In contrast, the others, which are called AZAP-family Arf GAPs, contain an Arf GAP domain following a pleckstrin homology (PH) domain in the middle of the protein. They are subdivided into four subfamilies, ASAPs, ACAPs, ARAPs, and AGAPs.ASAP1 is one of the best-characterized Arf GAPs. In addition to PH and Arf GAP domains, ASAP1 contains an N-terminal Bin, Amphiphysin, and Rvs167/Rvs161 (BAR) domain and, in the C-terminal half of the protein, a proline (Pro)-rich domain and Src homology 3 (SH3) domain. Other ASAP isoforms, ASAP2 and ASAP3, have similar domain structures and high homology, especially in the Arf GAP domains, although ASAP3 lacks C-terminal SH3 domain (Ha et al., 2008). Through its Pro-rich and SH3 domains, ASAP1 interacts with a number of proteins, which are mainly adhesion-and actin cytoskeleton-related proteins including Src, focal adhesion kinase (FAK), Crk/CrkL, and cortactin (Brown et al., 1998;Liu et al., 2002;Oda et al., 2003;Onodera et al., 2005;Bharti et al., 2007). ASAP1 is a component of three integrated membrane/actin cytoskeleton structures: focal adhesions, circular dorsal ruffles (CDRs) and invadopodia/podosomes. ASAP1 associates with focal adhesions in fibroblasts . The focal adhesion localization depends on the interaction of ASAP1 with FA...

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“…It was shown before that SHIP2 binds the E3 ligase Cbl and Cbl-associated protein (CAP) and SHIP2 is therefore suggested to have a role in endocytosis [29,35]. Furthermore, it was reported that Arap3 binds the adaptor protein CIN85 [13] and our screen identified the CIN85-related protein CMS as an Arap3 binding partner as well (Table 1). These two adaptor proteins both function in Cbl-mediated endocytosis [14].…”

Section: Discussionmentioning

confidence: 55%

“…Previously it was shown that Arap3 is present in a multimeric protein complex with the SH3 domain-containing protein CIN85 that binds Arap3 via a specific proline-arginine motif [13]. Our screen also identified the CIN85-related protein, CMS.…”

Section: Arap3 Is Part Of a Multimeric Protein Complexmentioning

confidence: 70%

“…Thus far, the function and the binding partner of the Arap3 SAM domain are unknown. Besides PI(3,4,5,)P 3 lipids and Rap1 GTP , the only known interaction partner for Arap3 is the adaptor protein CIN85 that is involved in the internalization of monoubiquitinated membrane proteins [13,14]. This interaction is mediated by a prolinearginine motif in Arap3 that is specific for the CIN85 SH3 domain (Fig.…”

Section: Introductionmentioning

confidence: 99%

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The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner

Raaijmakers

Deneubourg

Rehmann

et al. 2007

Cellular Signalling

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Arap3 is a phosphoinositide (PI) 3 kinase effector that serves as a GTPase activating protein (GAP) for both Arf and Rho G-proteins. The protein has multiple pleckstrin homology (PH) domains that bind preferentially phosphatidyl-inositol-3,4,5-trisphosphate (PI(3,4,5,)P 3 ) to induce translocation of Arap3 to the plasma membrane upon PI3K activation. Arap3 also contains a Ras association (RA) domain that interacts with the small G-protein Rap1 and a sterile alpha motif (SAM) domain of unknown function. In a yeast two-hybrid screen for new interaction partners of Arap3, we identified the PI 5′-phosphatase SHIP2 as an interaction partner of Arap3. The interaction between Arap3 and SHIP2 was observed with endogenous proteins and shown to be mediated by the SAM domain of Arap3 and SHIP2. In vitro, these two domains show specificity for a heterodimeric interaction. Since it was shown previously that Arap3 has a higher affinity for PI(3,4,5,)P 3 than for PI(3,4)P 2 , we propose that the SAM domain of Arap3 can function to recruit a negative regulator of PI3K signaling into the effector complex.

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CIN85 Associates with Multiple Effectors Controlling Intracellular Trafficking of Epidermal Growth Factor Receptors

Cited by 121 publications

References 65 publications

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner

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