DID2

Summary

Gene Symbol: DID2
Description: Did2p
Alias: CHM1, FTI1, VPL30, VPS46, Did2p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Nickerson D, West M, Henry R, Odorizzi G. Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol Biol Cell. 2010;21:1023-32 pubmed publisher
    ..b>Did2 plays a unique role in the regulation of MVB lumenal vesicle size, whereas Vtal and Vps60 promote efficient ..
  2. Azmi I, Davies B, Xiao J, Babst M, Xu Z, Katzmann D. ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1. Dev Cell. 2008;14:50-61 pubmed publisher
    ..Moreover, Did2 can stimulate Vps4 by both mechanisms in distinct contexts...
  3. Babst M, Katzmann D, Estepa Sabal E, Meerloo T, Emr S. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell. 2002;3:271-82 pubmed
    ..The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes. ..
  4. Shestakova A, Hanono A, Drosner S, Curtiss M, Davies B, Katzmann D, et al. Assembly of the AAA ATPase Vps4 on ESCRT-III. Mol Biol Cell. 2010;21:1059-71 pubmed publisher
    ..are mediated by a complex network of at least 12 distinct interactions between Vps4, ESCRT-III, Ist1, Vta1, and Did2. The order of events leading to active, ESCRT-III-associated Vps4 is poorly understood...
  5. Xiao J, Chen X, Davies B, Saltiel A, Katzmann D, Xu Z. Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis. Mol Biol Cell. 2009;20:3514-24 pubmed publisher
    ..Ist1NTD specifically binds to the ESCRT-III subunit Did2, and cocrystallization of Ist1NTD with a Did2 fragment shows that Ist1 interacts with the Did2 C-terminal MIM1 (MIT-..
  6. Obita T, Saksena S, Ghazi Tabatabai S, Gill D, Perisic O, Emr S, et al. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature. 2007;449:735-9 pubmed publisher
    ..Here we show that, of the six ESCRT--related subunits in yeast, only Vps2 and Did2 bind the MIT (microtubule interacting and transport) domain of Vps4, and that the carboxy-terminal 30 residues of ..
  7. Lottridge J, Flannery A, Vincelli J, Stevens T. Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body. Proc Natl Acad Sci U S A. 2006;103:6202-7 pubmed
    Previous two-hybrid analysis of the 17 soluble class E Vps yeast proteins revealed that Vps46p/Did2p interacts with Vta1p and the AAA (ATPase associated with a variety of cellular activities) ATPase Vps4p...
  8. Bowers K, Lottridge J, Helliwell S, Goldthwaite L, Luzio J, Stevens T. Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic. 2004;5:194-210 pubmed
    ..We propose the formation of a large multimeric complex on the endosome membrane consisting of ESCRTI, ESCRTII, ESCRTIII and other associated proteins. ..
  9. Amerik A, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol Cell. 2000;11:3365-80 pubmed

More Information

Publications21

  1. Nickerson D, West M, Odorizzi G. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J Cell Biol. 2006;175:715-20 pubmed
    ..We show that Did2 directs Vps4 activity to the dissociation of ESCRT-III but has no role in the dissociation of ESCRT-I or -II...
  2. Dimaano C, Jones C, Hanono A, Curtiss M, Babst M. Ist1 regulates Vps4 localization and assembly. Mol Biol Cell. 2008;19:465-74 pubmed
    ..data suggest that Ist1 has a dual role in the regulation of Vps4 activity: it localizes to the ESCRT machinery via Did2 where it positively regulates recruitment of Vps4 and it negatively regulates Vps4 by forming an Ist1-Vps4 ..
  3. Rue S, Mattei S, Saksena S, Emr S. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell. 2008;19:475-84 pubmed
    ..Moreover, this approach revealed that Ist1-Did2 and Vta1-Vps60 compose two functional units...
  4. Vajjhala P, Nguyen C, Landsberg M, Kistler C, Gan A, King G, et al. The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases. FEBS J. 2008;275:1427-49 pubmed publisher
    ..We propose that Vps4 SRH function requires an intact C-terminal helix. Co-evolution of a distinct Vps4 SRH and C-terminal helix in meiotic clade AAA ATPases supports this possibility. ..
  5. Vajjhala P, Wong J, To H, Munn A. The beta domain is required for Vps4p oligomerization into a functionally active ATPase. FEBS J. 2006;273:2357-73 pubmed
    ..Our studies suggest that assembly of a Vps4p oligomeric complex with full ATPase activity that interacts with Vta1p is essential for normal endosome function. ..
  6. Adell M, Vogel G, Pakdel M, M ller M, Lindner H, Hess M, et al. Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation. J Cell Biol. 2014;205:33-49 pubmed publisher
    ..Thus, Vps4 not only recycles ESCRT-III subunits but also cooperates with ESCRT-III to drive distinct membrane-remodeling steps, which lead to efficient membrane scission at the end of ILV biogenesis in vivo...
  7. Vajjhala P, Catchpoole E, Nguyen C, Kistler C, Munn A. Vps4 regulates a subset of protein interactions at the multivesicular endosome. FEBS J. 2007;274:1894-907 pubmed
    ..Our studies indicate that the MIT domain has a dual role in substrate binding and recruitment to endosomes and indicate that Vps4 disassembles the MVB sorting machinery by direct effects on multiple proteins. ..
  8. Weiss P, Huppert S, Kölling R. ESCRT-III protein Snf7 mediates high-level expression of the SUC2 gene via the Rim101 pathway. Eukaryot Cell. 2008;7:1888-94 pubmed publisher
    ..Furthermore, Snf7 turned out to be dispensable for SUC2 expression in an NRG1 deletion background. Thus, the effects of Snf7 on SUC2 expression can be completely accounted for by its effect on Nrg1 levels. ..
  9. Jones C, Ott E, Keener J, Curtiss M, Sandrin V, Babst M. Regulation of membrane protein degradation by starvation-response pathways. Traffic. 2012;13:468-82 pubmed publisher
    ..Together, the data indicate that protein synthesis and turnover are linked by a common regulatory system that ensures adaptation and survival under nutrient-stress conditions. ..
  10. Tong Z, Kim M, Pandey A, Espenshade P. Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast. Mol Cell Proteomics. 2014;13:2871-82 pubmed publisher
    ..This quantitative diGly proteomics methodology will serve as a robust platform for screening for stress conditions that require Tul1 E3 ligase activity. ..
  11. Haag C, Pohlmann T, Feldbrügge M. The ESCRT regulator Did2 maintains the balance between long-distance endosomal transport and endocytic trafficking. PLoS Genet. 2017;13:e1006734 pubmed publisher
    ..Here, we demonstrate that the ESCRT regulator Did2 coordinates endosomal transport in fungal hyphae of Ustilago maydis...
  12. Bauer I, Brune T, Preiss R, Kölling R. Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7. Genetics. 2015;201:1439-52 pubmed publisher