Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7
Download
10.1038.s41467-019-09437-x.pdf
Date
2019-03-29
Author
Sapmaz, Aysegul
Berlin, Ilana
Bos, Erik
Wijdeven, Ruud H.
Janssen, Hans
Konietzny, Rebecca
Akkermans, Jimmy J.
Erson Bensan, Ayşe Elif
Koning, Roman
Kessler, Benedikt M.
Neefjes, Jacques
Ovaa, Huib
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
198
views
134
downloads
Cite This
The endosomal system is a highly dynamic multifunctional organelle, whose complexity is regulated in part by reversible ubiquitylation. Despite the wide-ranging influence of ubiquitin in endosomal processes, relatively few enzymes utilizing ubiquitin have been described to control endosome integrity and function. Here we reveal the deubiquitylating enzyme (DUB) ubiquitin-specific protease 32 (USP32) as a powerful player in this context. Loss of USP32 inhibits late endosome (LE) transport and recycling of LE cargos, resulting in dispersion and swelling of the late compartment. Using SILAC-based ubiquitome profiling we identify the small GTPase Rab7-the logistical centerpiece of LE biology-as a substrate of USP32. Mechanistic studies reveal that LE transport effector RILP prefers ubiquitylation-deficient Rab7, while retromer-mediated LE recycling benefits from an intact cycle of Rab7 ubiquity-lation. Collectively, our observations suggest that reversible ubiquitylation helps switch Rab7 between its various functions, thereby maintaining global spatiotemporal order in the endosomal system.
Subject Keywords
General Biochemistry, Genetics and Molecular Biology
,
General Physics and Astronomy
,
General Chemistry
URI
https://hdl.handle.net/11511/40211
Journal
NATURE COMMUNICATIONS
DOI
https://doi.org/10.1038/s41467-019-09437-x
Collections
Department of Biology, Article
Suggestions
OpenMETU
Core
Cancer onset and progression: A genome-wide, nonlinear dynamical systems perspective on onconetworks
Qu, K.; Haidar, A. Abi; Fan, J.; Ensman, L.; Tuncay, Kağan; Jolly, M.; Ortoleva, P. (Elsevier BV, 2007-05-21)
It is hypothesized that the many human cell types corresponding to multiple states is supported by an underlying nonlinear dynamical system (NDS) of transcriptional regulatory network (TRN) processes. This hypothesis is validated for epithelial cells whose TRN is found to support an extremely complex array of states that we term a "bifurcation nexus", for which we introduce a quantitative measure of complexity. The TRN used is constructed and analyzed by integrating a database of TRN information, cDNA micro...
Trehalose glycopolymer resists allow direct writing of protein patterns by electron-beam lithography
Bat, Erhan; Lau, Uland Y.; Maynard, Heather D. (Springer Science and Business Media LLC, 2015-03-01)
Direct-write patterning of multiple proteins on surfaces is of tremendous interest for a myriad of applications. Precise arrangement of different proteins at increasingly smaller dimensions is a fundamental challenge to apply the materials in tissue engineering, diagnostics, proteomics and biosensors. Herein, we present a new resist that protects proteins during electron-beam exposure and its application in direct-write patterning of multiple proteins. Polymers with pendant trehalose units are shown to effe...
Structural Basis for EPC1-Mediated Recruitment of MBTD1 into the NuA4/TIP60 Acetyltransferase Complex
Zhang, Heng; Devoucoux, Maëva; Song, Xiaosheng; Li, Li; Ayaz, Gamze; Cheng, Harry; Tempel, Wolfram; Dong, Cheng; Loppnau, Peter; Côté, Jacques; Min, Jinrong (Elsevier BV, 2020-3)
MBTD1, a H4K20me reader, has recently been identified as a component of the NuA4/TIP60 acetyltransferase complex, regulating gene expression and DNA repair. NuA4/TIP60 inhibits 53BP1 binding to chromatin through recognition of the H4K20me mark by MBTD1 and acetylation of H2AK15, blocking the ubiquitination mark required for 53BP1 localization at DNA breaks. The NuA4/TIP60 non-catalytic subunit EPC1 enlists MBTD1 into the complex, but the detailed molecular mechanism remains incompletely explored. Here, we p...
1SR,2SR,3SR,4RS,5RS,6RS,7SR,8RS)-7,8-dichlorobicyclo[4.2.0]octa-2,3,4,5-tetrayl tetraacetate
Sahin, Ertan; Kelebekli, Latif; Kara, Yunus; Balcı, Metin (International Union of Crystallography (IUCr), 2006-07-01)
In the title compound, C16H20Cl2O8, the bicyclic system contains a central non-planar cyclohexane ring which is fused to a cyclobutane moiety. The cyclohexane ring has a chair conformation and the whole system adopts a syn conformation. The structure provides information on the stereochemical course of the chlorination, photo-oxidation and hydroxylation steps of the reaction.
GOPred: GO Molecular Function Prediction by Combined Classifiers
Sarac, Oemer Sinan; Atalay, Mehmet Volkan; Atalay, Rengül (Public Library of Science (PLoS), 2010-08-31)
Functional protein annotation is an important matter for in vivo and in silico biology. Several computational methods have been proposed that make use of a wide range of features such as motifs, domains, homology, structure and physicochemical properties. There is no single method that performs best in all functional classification problems because information obtained using any of these features depends on the function to be assigned to the protein. In this study, we portray a novel approach that combines ...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
A. Sapmaz et al., “USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7,”
NATURE COMMUNICATIONS
, pp. 0–0, 2019, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/40211.