Keyword search (4,164 papers available)

"Milev MP" Authored Publications:

Title Authors PubMed ID
1 SEC24C deficiency causes trafficking and glycosylation abnormalities in an epileptic encephalopathy with cataracts and dyserythropoeisis Bögershausen N; Cavdarli B; Nagai T; Milev MP; Wolff A; Mehranfar M; Schmidt J; Choudhary D; Gutiérrez-Gutiérrez Ó; Cyganek L; Saint-Dic D; Zibat A; Köhrer K; Wollenweber TE; Wieczorek D; Altmüller J; Borodina T; Kaçar D; Haliloglu G; Li Y; Thiel C; Sacher M; Knapik EW; Yigit G; Wollnik B; 40131364
BIOLOGY
2 A Humanized Yeast Model for Studying TRAPP Complex Mutations; Proof-of-Concept Using Variants from an Individual with a TRAPPC1-Associated Neurodevelopmental Syndrome Zykaj E; Abboud C; Asadi P; Warsame S; Almousa H; Milev MP; Greco BM; López-Sánchez M; Bratkovic D; Kachroo AH; Pérez-Jurado LA; Sacher M; 39273027
BIOLOGY
3 Dynamic regulation of inter-organelle communication by ubiquitylation controls skeletal muscle development and disease onset Mansur A; Joseph R; Kim ES; Jean-Beltran PM; Udeshi ND; Pearce C; Jiang H; Iwase R; Milev MP; Almousa HA; McNamara E; Widrick J; Perez C; Ravenscroft G; Sacher M; Cole PA; Carr SA; Gupta VA; 37432316
BIOLOGY
4 Vitamin B5, a Coenzyme A precursor, rescues TANGO2 deficiency disease-associated defects in Drosophila and human cells Asadi P; Milev MP; Saint-Dic D; Gamberi C; Sacher M; 36502486
BIOLOGY
5 Biallelic variants in TRAPPC10 cause a microcephalic TRAPPopathy disorder in humans and mice Rawlins LE; Almousa H; Khan S; Collins SC; Milev MP; Leslie J; Saint-Dic D; Khan V; Hincapie AM; Day JO; McGavin L; Rowley C; Harlalka GV; Vancollie VE; Ahmad W; Lelliott CJ; Gul A; Yalcin B; Crosby AH; Sacher M; Baple EL; 35298461
BIOLOGY
6 TRAPPC11-related muscular dystrophy with hypoglycosylation of alpha-dystroglycan in skeletal muscle and brain Munot P; McCrea N; Torelli S; Manzur A; Sewry C; Chambers D; Feng L; Ala P; Zaharieva I; Ragge N; Roper H; Marton T; Cox P; Milev MP; Liang WC; Maruyama S; Nishino I; Sacher M; Phadke R; Muntoni F; 34648194
BIOLOGY
7 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
8 The phenotype associated with variants in TANGO2 may be explained by a dual role of the protein in ER-to-Golgi transport and at the mitochondria. Milev MP, Saint-Dic D, Zardoui K, Klopstock T, Law C, Distelmaier F, Sacher M 32909282
BIOLOGY
9 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
10 Mutations in TRAPPC12 Manifest in Progressive Childhood Encephalopathy and Golgi Dysfunction. Milev MP, Grout ME, Saint-Dic D, Cheng YH, Glass IA, Hale CJ, Hanna DS, Dorschner MO, Prematilake K, Shaag A, Elpeleg O, Sacher M, Doherty D, Edvardson S 28777934
BIOLOGY
11 TRAMM/TrappC12 plays a role in chromosome congression, kinetochore stability, and CENP-E recruitment. Milev MP, Hasaj B, Saint-Dic D, Snounou S, Zhao Q, Sacher M 25918224
BIOLOGY
12 TRAPPC11 and GOSR2 mutations associate with hypoglycosylation of α-dystroglycan and muscular dystrophy. Larson AA, Baker PR, Milev MP, Press CA, Sokol RJ, Cox MO, Lekostaj JK, Stence AA, Bossler AD, Mueller JM, Prematilake K, Tadjo TF, Williams CA, Sacher M, Moore SA 29855340
BIOLOGY
13 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
14 TRAPPopathies: An emerging set of disorders linked to variations in the genes encoding transport protein particle (TRAPP)-associated proteins. Sacher M, Shahrzad N, Kamel H, Milev MP 30152084
BIOLOGY
15 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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