Recruitment of Tom1L1/Srcasm to Endosomes and the Midbody by Tsg101

Yanagida-Ishizaki, Yuko; Takei, Tomomi; Ishizaki, Ray; Imakagura, Hitoshi; Takahashi, Shouji; Shin, Hye‐Won; Katoh, Yohei; Nakayama, Kazuhisa

doi:10.1247/csf.07037

Cited by 22 publications

(22 citation statements)

References 34 publications

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“…Recent studies have identified the presence of endosomal proteins including endosomal sorting complex required for transport proteins and Tom1L1 at the midbody during cytokinesis in which they function as regulators of mitotic cell division (Morita et al, 2007;Yanagida-Ishizaki et al, 2008). Interestingly, we observed that endogenous Vav2 protein localized to the central spindles of mitotic cells at telophase stage as well as at the midbody during cytokinesis in which it co-localized with the Tom1L1 protein (Thalappilly and Dusetti, unpublished results).…”

Section: Vav2 Regulates Egfr Stability S Thalappilly Et Almentioning

confidence: 52%

VAV2 regulates epidermal growth factor receptor endocytosis and degradation

et al. 2010

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Vav proteins are guanine nucleotide exchange factors for Rho GTPases that regulate cell adhesion, motility, spreading and proliferation in response to growth factor signalling. In this work, we show that Vav2 expression delayed epidermal growth factor receptor (EGFR) internalization and degradation, and enhanced EGFR, ERK and Akt phosphorylations. This effect of Vav2 on EGFR degradation is dependent on its guanine nucleotide exchange function. Knockdown of Vav2 in HeLa cells enhanced EGFR degradation and reduced cell proliferation. epidermal growth factor stimulation led to colocalization of Vav2 with EGFR and Rab5 in endosomes. We further show that the effect of Vav2 on EGFR stability is modulated by its interaction with two endosome-associated proteins and require RhoA function. Thus, in this work, we report for the first time that Vav2 can regulate growth factors receptor signalling by slowing receptor internalization and degradation through its interaction with endosome-associated proteins.

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Section: Vav2 Regulates Egfr Stability S Thalappilly Et Almentioning

confidence: 52%

VAV2 regulates epidermal growth factor receptor endocytosis and degradation

et al. 2010

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“…Although all Tom1 family members are capable of interacting with the ESCRT-0 component Hrs, only Tom1L1 interacts with the ESCRT-I component TSG101. Moreover, only Tom1 can associate with endofin, suggesting that the family members have both redundant and unique functions (Puertollano, 2005;Seet et al, 2004;Yanagida-Ishizaki et al, 2008). Further divergence in the Tom1 family occurs within the C-terminal region, in which Tom1 and Tom1L2 are most similar, whereas Tom1L1 shows less similarity (Fig.…”

Section: Cargo Sorting In the Endocytic Pathwaymentioning

confidence: 98%

Myosin VI and its cargo adaptors – linking endocytosis and autophagy

Tumbarello

Kendrick‐Jones

Buß

2013

Journal of Cell Science

117

127

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SummaryThe coordinated trafficking and tethering of membrane cargo within cells relies on the function of distinct cytoskeletal motors that are targeted to specific subcellular compartments through interactions with protein adaptors and phospholipids. The unique actin motor myosin VI functions at distinct steps during clathrin-mediated endocytosis and the early endocytic pathway -both of which are involved in cargo trafficking and sorting -through interactions with Dab2, GIPC, Tom1 and LMTK2. This multifunctional ability of myosin VI can be attributed to its cargo-binding tail region that contains two protein-protein interaction interfaces, a ubiquitin-binding motif and a phospholipid binding domain. In addition, myosin VI has been shown to be a regulator of the autophagy pathway, because of its ability to link the endocytic and autophagic pathways through interactions with the ESCRT-0 protein Tom1 and the autophagy adaptor proteins T6BP, NDP52 and optineurin. This function has been attributed to facilitating autophagosome maturation and subsequent fusion with the lysosome. Therefore, in this Commentary, we discuss the relationship between myosin VI and the different myosin VI adaptor proteins, particularly with regards to the spatial and temporal regulation that is required for the sorting of cargo at the early endosome, and their impact on autophagy.

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“…The ESCRT 0 components Vps27 and Hse1 are both VHS domain-containing proteins, as are the Tom1 protein family (Puertollano, 2005;Raiborg and Stenmark, 2009). Recent evidence has been presented, in multiple and diverse eukaryotes, that Tom1 and related proteins bind ubiquitylated cargo (Blanc et al, 2009;Katoh et al, 2004) and the ESCRT I component Tsg101/Vps23 (Yanagida-Ishizaki et al, 2008). Consequently, it has been proposed that Tom1 proteins might have a role as central components of an ancient alternative ESCRT 0 machinery (Blanc et al, 2009).…”

Section: Tom1 Evolutionmentioning

confidence: 99%

“…The latter sequence-based approach was expanded to explore the representation of ESCRT machinery in available amoebozoan genomic databases. Recent evidence raised the possibility of an alternative ESCRT-0-like machinery centered on the Tom1 protein family (Blanc et al, 2009;Yanagida-Ishizaki et al, 2008). Tom1 family homologs have been identified in opisthokonts, as well as in Dictyostelium discoideum and the multicellular plants Arabidopsis thaliana and Oryza sativa (Blanc et al, 2009;Winter and Hauser, 2006).…”

mentioning

confidence: 99%

Multivesicular bodies in the enigmatic amoeboflagellateBreviata anathemaand the evolution of ESCRT 0

Herman

Walker

Giezen

et al. 2011

Journal of Cell Science

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Endosomal sorting complexes required for transport (ESCRTs) are heteromeric protein complexes required for multivesicular body (MVB) morphogenesis. ESCRTs I, II, III and III-associated are ubiquitous in eukaryotes and presumably ancient in origin. ESCRT 0 recruits cargo to the MVB and appears to be opisthokont-specific, bringing into question aspects of the current model of ESCRT mechanism. One caveat to the restricted distribution of ESCRT 0 was the previous limited availability of amoebozoan genomes, the supergroup closest to opisthokonts. Here, we significantly expand the sampling of ESCRTs in Amoebozoa. Our electron micrographic and bioinformatics evidence confirm the presence of MVBs in the amoeboflagellate Breviata anathema. Searches of genomic databases of amoebozoans confirm the ubiquitous nature of ESCRTs I–III-associated and the restriction of ESCRT 0 to opisthokonts. Recently, an alternate ESCRT 0 complex, centering on Tom1 proteins, has been proposed. We determine the distribution of Tom1 family proteins across eukaryotes and show that the Tom1, Tom1L1 and Tom1L2 proteins are a vertebrate-specific expansion of the single Tom1 family ancestor, which has indeed been identified in at least one member of each of the major eukaryotic supergroups. This implies a more widely conserved and ancient role for the Tom1 family in endocytosis than previously suspected.

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Recruitment of Tom1L1/Srcasm to Endosomes and the Midbody by Tsg101

Cited by 22 publications

References 34 publications

VAV2 regulates epidermal growth factor receptor endocytosis and degradation

VAV2 regulates epidermal growth factor receptor endocytosis and degradation

Myosin VI and its cargo adaptors – linking endocytosis and autophagy

Multivesicular bodies in the enigmatic amoeboflagellateBreviata anathemaand the evolution of ESCRT 0

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