Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5.

Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Research Abstract Details 

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Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Abstract Text:

Andrea J Oestreich,Mariam Aboian,Jacqueline Lee,Ishara Azmi,Johanna Payne,Rachel Issaka,Brian A Davies,David J Katzmann,

A subset of proteins that transit the endosomal system are directed into the intralumenal vesicles of multivesicular bodies (MVBs). MVB formation is critical for a variety of cellular functions including receptor down-regulation, viral budding, antigen presentation, and the generation of lysosome-related organelles. Entry of transmembrane proteins into the intralumenal vesicles of a MVB is a highly regulated process that is positively modulated by covalent modification of cargoes with ubiquitin. To identify additional MVB sorting signals, we examined the previously described ubiquitination-independent MVB cargo Sna3. Although Sna3 ubiquitination is not essential, Sna3 MVB sorting is positively modulated by its ubiquitination. Examination of MVB sorting determinants within a form of Sna3 lacking all lysine residues identified two critical regions: an amino-terminal tyrosine-containing region and a carboxyl-terminal PPAY motif. This PPAY motif interacts with the WW domains of the ubiquitin ligase Rsp5, and mutations in either the WW or, surprisingly, the HECT domains of Rsp5 negatively impacted MVB targeting of lysine-minus Sna3. These data indicate that Rsp5 function is required for MVB targeting of Sna3 in a capacity beyond cargo ubiquitination. These results uncover a series of determinants impacting Sna3 MVB sorting, including unexpected roles for Rsp5.

Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Publishing Authors By Initials

AJ Oestreich,M Aboian,J Lee,I Azmi,J Payne,R Issaka,BA Davies,DJ Katzmann,

For similar enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes research abstracts see: enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes research

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Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular biology of the cell

VOLUME: 18

Page Numbers: 707-20

Journal Abbreviation: Mol. Biol. Cell

ISSN: 1059-1524

DAY: 20

MONTH: 12

YEAR: 2006

Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Information

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LANGUAGE: eng

NlmUniqueID: 9201390

Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Keywords Mesh Terms:

KEYWORDS: Ubiquitin-Protein Ligase Complexes

MESH TERMS: metabolism

Chemical & Substance for Abstract: Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Information

Substance Name: Ubiquitin-Protein Ligase Complexes

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5.

AFFILIATION: Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM 73024-1

ACRONYM: GM

MEDLINETA: Mol Biol Cell

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