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TRAMM/TrappC12 plays a role in chromosome congression, kinetochore stability, and CENP-E recruitment.

Author(s): Milev MP, Hasaj B, Saint-Dic D, Snounou S, Zhao Q, Sacher M

J Cell Biol. 2015 Apr 27;209(2):221-34 Authors: Milev MP, Hasaj B, Saint-Dic D, Snounou S, Zhao Q, Sacher M

Article GUID: 25918224
TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes.

Author(s): Stanga D, Zhao Q, Milev MP, Saint-Dic D, Jimenez-Mallebrera C, Sacher M

Traffic. 2019 May;20(5):325-345 Authors: Stanga D, Zhao Q, Milev MP, Saint-Dic D, Jimenez-Mallebrera C, Sacher M

Article GUID: 30843302
Title:TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes.
Authors:Stanga D,  Zhao Q,  Milev MP,  Saint-Dic D,  Jimenez-Mallebrera C,  Sacher M
Link:https://www.ncbi.nlm.nih.gov/pubmed/30843302?dopt=Abstract
Category:Traffic
PMID:30843302
Dept Affiliation: CONCORDIA
1 Concordia University, Department of Biology, Montreal, Quebec, Canada.
2 University of Montreal, Department of Medicine and Institute for Research in Immunology and Cancer, Montreal, Quebec, Canada.
3 Neuromuscular Unit, Neuropaediatrics Department, Institut de Recerca Sant Joan de Déu, Hospital Sant Joan de Déu and CIBERER, Barcelona, Spain.
4 McGill University, Department of Anatomy and Cell Biology, Quebec, Canada.

Description:

TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes.

Traffic. 2019 May;20(5):325-345

Authors: Stanga D, Zhao Q, Milev MP, Saint-Dic D, Jimenez-Mallebrera C, Sacher M

Abstract

TRAPPC11 has been implicated in membrane traffic and lipid-linked oligosaccharide synthesis, and mutations in TRAPPC11 result in neuromuscular and developmental phenotypes. Here, we show that TRAPPC11 has a role upstream of autophagosome formation during macroautophagy. Upon TRAPPC11 depletion, LC3-positive membranes accumulate prior to, and fail to be cleared during, starvation. A proximity biotinylation assay identified ATG2B and its binding partner WIPI4/WDR45 as TRAPPC11 interactors. TRAPPC11 depletion phenocopies that of ATG2 and WIPI4 and recruitment of both proteins to membranes is defective upon reduction of TRAPPC11. We find that a portion of TRAPPC11 and other TRAPP III proteins localize to isolation membranes. Fibroblasts from a patient with TRAPPC11 mutations failed to recruit ATG2B-WIPI4, suggesting that this interaction is physiologically relevant. Since ATG2B-WIPI4 is required for isolation membrane expansion, our study suggests that TRAPPC11 plays a role in this process. We propose a model whereby the TRAPP III complex participates in the formation and expansion of the isolation membrane at several steps.

PMID: 30843302 [PubMed - in process]