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Volumn 15, Issue 4, 2003, Pages 446-455

Protein sorting into multivesicular endosomes

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; MEMBRANE PROTEIN; PROTEIN HRS; PROTEIN VPS27; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0042174019     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00080-2     Document Type: Review
Times cited : (423)

References (68)
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    • The class E Vps proteins Vps22, Vps25 and Vps36 are shown to assemble into a 155 kDa protein complex, ESCRT-II. It acts downstream of the previously described ESCRT-I complex [24] and is transiently associated with endosomal membranes. Immunoprecipitation experiments indicate that components of ESCRT-II can interact with components of ESCRT-III, and subunits of ESCRT-III become more cytosolic in cells that lack ESCRT-II components. The authors suggest that ESCRT-II can initiate the formation of ESCRT-III on endosomal membranes.
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    • •]), the authors continue their investigation of the structure of this domain in complex with the HIV late-domain PTAP sequence. Interestingly, a similar motif (PSAP) is found in Hrs.
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    • This report shows that the V40 protein from Ebola virus can interact with human Nedd4 and Tsg101 in vitro. The WW domain 3 of Nedd4 is necessary and sufficient for binding to the PPXY motif of V40, whereas the UEV domain of Tsg101 is sufficient to bind the PTAP domain of the virus protein.
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    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Mutational analysis of the PTAPPEY sequence indicates that the PTAP and PPEY motifs can function separately in virus budding, and the PTAP motif recruits Tsg101 into the virus buds. Furthermore, a dominant-negative mutant of Vps4 inhibits the budding of the Ebola virus.
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    • The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4
    • This study gives another intriguing example of how viruses can induce endocytic downregulation of host proteins, thereby evading the cellular immune response.
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    • Chen L., Davis N.G. Ubiquitin-independent entry into the yeast recycling pathway. Traffic. 3:2002;110-123 In this report, trafficking of the yeast a-factor receptor Ste3p is investigated. While the constitutive ligand-independent uptake and vacuolar degradation of the receptor are dependent on receptor ubiquitination, ligand-dependent internalisation and recycling are not.
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    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • •] show evidence that receptors for epidermal growth factor and platelet-derived growth factor become multiply monoubiquitinated (and not polyubiquitinated) upon ligand binding. A single attached ubiquitin appears to be sufficient for endocytosis and lysosomal degradation.
    • •] show evidence that receptors for epidermal growth factor and platelet-derived growth factor become multiply monoubiquitinated (and not polyubiquitinated) upon ligand binding. A single attached ubiquitin appears to be sufficient for endocytosis and lysosomal degradation.
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    • Endocytosis of receptor tyrosine kinases is driven by mono-, not poly-, ubiquitylation
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    • Endosomal dynamics of met determine signaling output
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    • Hammond D.E., Carter S., McCullough J., Urbe S., Vande W.G., Clague M.J. Endosomal dynamics of met determine signaling output. Mol. Biol. Cell. 14:2003;1346-1354 The proteasomal inhibitor lactacystin alters the routing of the endocytosed hepatocyte growth factor receptor (Met). Lactacystin causes the endocytosed receptor to recycle to the plasma membrane instead of being degraded in lysosomes, and phosphorylation of the receptor is prevented. Reduction of cellular Hrs levels retards degradation and dephosphorylation of Met.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.