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Syntaxin 5 Is Required for the Formation and Clearance of Protein Inclusions during Proteostatic Stress

Journal article
Authors Roja Babazadeh
Doryaneh Ahmadpour
S. Jia
Xinxin Hao
Per O Widlund
Kara Schneider
Frederik Eisele
L. D. Edo
G. J. Smits
Liu Beidong
Thomas Nyström
Published in Cell Reports
Volume 28
Issue 8
Pages 2096-+
ISSN 2211-1247
Publication year 2019
Published at Institute of Biomedicine
Institute of Biomedicine, Department of Microbiology and Immunology
Department of Chemistry and Molecular Biology
Pages 2096-+
Language en
Links dx.doi.org/10.1016/j.celrep.2019.07...
Keywords asymmetric inheritance, damaged proteins, quality-control, saccharomyces-cerevisiae, endoplasmic-reticulum, molecular chaperones, misfolded proteins, spatial sequestration, retrograde transport, golgi, morphology, Cell Biology
Subject categories Cell biology

Abstract

Spatial sorting to discrete quality control sites in the cell is a process harnessing the toxicity of aberrant proteins. We show that the yeast t-snare phosphoprotein syntaxin5 (Sed5) acts as a key factor in mitigating proteotoxicity and the spatial deposition and clearance of IPOD (insoluble protein deposit) inclusions associates with the disaggregase Hsp104. Sed5 phosphorylation promotes dynamic movement of COPII-associated Hsp104 and boosts disaggregation by favoring anterograde ER-to-Golgi trafficking. Hsp104-associated aggregates co-localize with Sed5 as well as components of the ER, trans Golgi network, and endocytic vesicles, transiently during proteostatic stress, explaining mechanistically how misfolded and aggregated proteins formed at the vicinity of the ER can hitchhike toward vacuolar IPOD sites. Many inclusions become associated with mitochondria in a HOPS/vCLAMP-dependent manner and co-localize with Vps39 (HOPS/vCLAMP) and Vps13, which are proteins providing contacts between vacuole and mitochondria. Both Vps39 and Vps13 are required also for efficient Sed5-dependent clearance of aggregates.

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