Source:http://linkedlifedata.com/resource/pubmed/id/17604280
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
2007-8-20
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pubmed:databankReference | |
pubmed:abstractText |
A mechanism by which ubiquitinated cargo proteins are sorted into multivesicular bodies (MVBs) from plasma and trans-Golgi network (TGN) membranes is well established in yeast and mammalian somatic cells. However, the ubiquitin-dependent sorting pathway has not been clearly defined in germ cells. In this study we identified a novel member of the transmembrane RING-finger family of proteins, termed membrane-associated RING-CH (MARCH)-XI, that is expressed predominantly in developing spermatids and weakly in brain and pituitary. MARCH-XI possesses an E3 ubiquitin ligase activity that targets CD4 for ubiquitination. Immunoelectron microscopy of rat round spermatids showed that MARCH-XI is localized to TGN-derived vesicles and MVBs. Fluorescence staining of rat round spermatids and immunoprecipitation of rat testis demonstrated that MARCH-XI forms complexes with the adaptor protein complex-1 and with fucose-containing glycoproteins including ubiquitinated forms. Furthermore, the C-terminal region of MARCH-XI mediates its interaction with mu1-adaptin and Veli through a tyrosine-based motif and a PDZ binding motif, respectively. Our data suggest that MARCH-XI acts as a ubiquitin ligase with a role in ubiquitin-mediated protein sorting in the TGN-MVB transport pathway, which may be involved in mammalian spermiogenesis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:FukudaHidekazuH,
pubmed-author:HirataYukioY,
pubmed-author:HiroseShigehisaS,
pubmed-author:KatoAkiraA,
pubmed-author:MorokumaYuriY,
pubmed-author:NakamuraNobuhiroN,
pubmed-author:NotoyaMichitakaM,
pubmed-author:SakaiYasuhiroY,
pubmed-author:YamamotoYokoY,
pubmed-author:YamashinaShoheiS
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24806-15
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pubmed:meshHeading |
pubmed-meshheading:17604280-Amino Acid Motifs,
pubmed-meshheading:17604280-Amino Acid Sequence,
pubmed-meshheading:17604280-Animals,
pubmed-meshheading:17604280-Brain,
pubmed-meshheading:17604280-Cloning, Molecular,
pubmed-meshheading:17604280-Male,
pubmed-meshheading:17604280-Microscopy, Immunoelectron,
pubmed-meshheading:17604280-Molecular Sequence Data,
pubmed-meshheading:17604280-Pituitary Gland,
pubmed-meshheading:17604280-Protein Binding,
pubmed-meshheading:17604280-Rats,
pubmed-meshheading:17604280-Recombinant Proteins,
pubmed-meshheading:17604280-Spermatids,
pubmed-meshheading:17604280-Ubiquitin,
pubmed-meshheading:17604280-Ubiquitin-Protein Ligases
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pubmed:year |
2007
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pubmed:articleTitle |
MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-dependent protein sorting in developing spermatids.
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pubmed:affiliation |
Department of Biological Sciences, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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