Keyword search (4,164 papers available)

"Stanga D" Authored Publications:

Title Authors PubMed ID
1 A Spike-Accum bioconjugate protein vaccine confers potent SARS-CoV-2-specific immunity Pierre Bikorimana J; Caveney NA; El-Hachem N; Mandl GA; Capobianco JA; Stanga D; Abusarah J; Hancock MA; Farah R; Gonçalves MP; Falzarano D; Liao M; Hamonic G; Liu Q; Beaudoin S; Talbot S; Rafei M; 41054531
CNSR
2 Publisher Correction: Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein. Milev MP; Stanga D; Schänzer A; Nascimento A; Saint-Dic D; Ortez C; Natera-de Benito D; Barrios DG; Colomer J; Badosa C; Jou C; Gallano P; Gonzalez-Quereda L; Töpf A; Johnson K; Straub V; Hahn A; Sacher M; Jimenez-Mallebrera C; 33173071
BIOLOGY
3 TRAPPing a neurological disorder: from yeast to humans. Lipatova Z, Van Bergen N, Stanga D, Sacher M, Christodoulou J, Segev N 32116085
BIOLOGY
4 Deficiencies in vesicular transport mediated by TRAPPC4 are associated with severe syndromic intellectual disability. Van Bergen NJ, Guo Y, Al-Deri N, Lipatova Z, Stanga D, Zhao S, Murtazina R, Gyurkovska V, Pehlivan D, Mitani T, Gezdirici A, Antony J, Collins F, Willis MJH, Coban Akdemir ZH, Liu P, Punetha J, Hunter JV, Jhangiani SN, Fatih JM, Rosenfeld JA, Posey JE, Gibbs RA, Karaca E, Massey S, Ranasinghe TG, Sleiman P, Troedson C, Lupski JR, Sacher M, Segev N, Hakonarson H, Christodoulou J 31794024
BIOLOGY
5 Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein. Milev MP, Stanga D, Schänzer A, Nascimento A, Saint-Dic D, Ortez C, Benito DN, Barrios DG, Colomer J, Badosa C, Jou C, Gallano P, Gonzalez-Quereda L, Töpf A, Johnson K, Straub V, Hahn A, Sacher M, Jimenez-Mallebrera C 31575891
BIOLOGY
6 Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts. Milev MP, Graziano C, Karall D, Kuper WFE, Al-Deri N, Cordelli DM, Haack TB, Danhauser K, Iuso A, Palombo F, Pippucci T, Prokisch H, Saint-Dic D, Seri M, Stanga D, Cenacchi G, van Gassen KLI, Zschocke J, Fauth C, Mayr JA, Sacher M, van Hasselt PM 30120216
BIOLOGY
7 TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes. Stanga D, Zhao Q, Milev MP, Saint-Dic D, Jimenez-Mallebrera C, Sacher M 30843302
CONCORDIA

 

Title:TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes.
Authors:Stanga DZhao QMilev MPSaint-Dic DJimenez-Mallebrera CSacher M
Link:https://www.ncbi.nlm.nih.gov/pubmed/30843302?dopt=Abstract
Publication:
Keywords:
PMID:30843302 Category:Traffic Date Added:2019-06-07
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]





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