Basolateral Endocytic Recycling Requires RAB-10 and AMPH-1 Mediated Recruitment of RAB-5 GAP TBC-2 to Endosomes

Ou Liu, Barth Grant

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The small GTPase RAB-5/Rab5 is a master regulator of the early endosome, required for a myriad of coordinated activities, including the degradation and recycling of internalized cargo. Here we focused on the recycling function of the early endosome and the regulation of RAB-5 by GAP protein TBC-2 in the basolateral C. elegans intestine. We demonstrate that downstream basolateral recycling regulators, GTPase RAB-10/Rab10 and BAR domain protein AMPH-1/Amphiphysin, bind to TBC-2 and help to recruit it to endosomes. In the absence of RAB-10 or AMPH-1 binding to TBC-2, RAB-5 membrane association is abnormally high and recycling cargo is trapped in early endosomes. Furthermore, the loss of TBC-2 or AMPH-1 leads to abnormally high spatial overlap of RAB-5 and RAB-10. Taken together our results indicate that RAB-10 and AMPH-1 mediated down-regulation of RAB-5 is an important step in recycling, required for cargo exit from early endosomes and regulation of early endosome–recycling endosome interactions.

Original languageEnglish (US)
Article numbere1005514
JournalPLoS genetics
Volume11
Issue number9
DOIs
StatePublished - Jan 1 2015

Fingerprint

endosomes
Endosomes
recycling
Recycling
cargo
guanosinetriphosphatase
protein
GTPase-activating proteins
GTPase-Activating Proteins
Monomeric GTP-Binding Proteins
GTP Phosphohydrolases
Intestines
membrane
intestines
Down-Regulation
degradation
Membranes
regulation
proteins

All Science Journal Classification (ASJC) codes

  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics
  • Genetics(clinical)
  • Cancer Research

Cite this

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Basolateral Endocytic Recycling Requires RAB-10 and AMPH-1 Mediated Recruitment of RAB-5 GAP TBC-2 to Endosomes. / Liu, Ou; Grant, Barth.

In: PLoS genetics, Vol. 11, No. 9, e1005514, 01.01.2015.

Research output: Contribution to journalArticle

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