The BLOC-1 complex promotes endosomal maturation by recruiting the Rab5 GTPase-activating protein Msb3

Autor(en): Peter, Arun T. John
Lachmann, Jens
Rana, Meenakshi
Bunge, Madeleine
Cabrera, Margarita
Ungermann, Christian 
Stichwörter: ARCHITECTURE; BIOGENESIS; CARGO; Cell Biology; GAP; GENE; HERMANSKY-PUDLAK-SYNDROME; IDENTIFICATION; ORGANELLES; TERMINATION; TRAFFICKING
Erscheinungsdatum: 2013
Herausgeber: ROCKEFELLER UNIV PRESS
Journal: JOURNAL OF CELL BIOLOGY
Volumen: 201
Ausgabe: 1
Startseite: 97
Seitenende: 111
Zusammenfassung: 
Membrane microcompartments of the early endosomes serve as a sorting and signaling platform, where receptors are either recycled back to the plasma membrane or forwarded to the lysosome for destruction. In metazoan cells, three complexes, termed BLOC-1 to -3, mediate protein sorting from the early endosome to lysosomes and lysosome-related organelles. We now demonstrate that BLOC-1 is an endosomal Rab-GAP (GTPase-activating protein) adapter complex in yeast. The yeast BLOC-1 consisted of six subunits, which localized interdependently to the endosomes in a Rab5/Vps21 dependent manner. In the absence of BLOC-1 subunits, the balance between recycling and degradation of selected cargoes was impaired. Additionally, our data show that BLOC-1 is both a Vps21 effector and an adapter for its GAP Msb3. BLOC-1 and Msb3 interacted in vivo, and both mutants resulted in a redistribution of active Vps21 to the vacuole surface. We thus conclude that BLOC-1 controls the lifetime of active Rab5/Vps21 and thus endosomal maturation along the endocytic pathway.
ISSN: 00219525
DOI: 10.1083/jcb.201210038

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