Endosomal recruitment of the WASH complex: Active sequences and mutations impairing interaction with the retromer
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Endosomal recruitment of the WASH complex: Active sequences and mutations impairing interaction with the retromer
Authors
Keywords
-
Journal
BIOLOGY OF THE CELL
Volume 105, Issue 5, Pages 191-207
Publisher
Wiley
Online
2013-01-18
DOI
10.1111/boc.201200038
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer
- (2012) Da Jia et al. MOLECULAR BIOLOGY OF THE CELL
- Actin Polymerization Controls the Organization of WASH Domains at the Surface of Endosomes
- (2012) Emmanuel Derivery et al. PLoS One
- Recruitment of the endosomal WASH complex is mediated by the extended ‘tail’ of Fam21 binding to the retromer protein Vps35
- (2011) Michael E. Harbour et al. BIOCHEMICAL JOURNAL
- SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless
- (2011) Peng Zhang et al. CELL RESEARCH
- Retromer Controls Epithelial Cell Polarity by Trafficking the Apical Determinant Crumbs
- (2011) Shirin Meher Pocha et al. CURRENT BIOLOGY
- Retromer regulates apical–basal polarity through recycling crumbs
- (2011) Bo Zhou et al. DEVELOPMENTAL BIOLOGY
- Actin polymerization driven by WASH causes V-ATPase retrieval and vesicle neutralization before exocytosis
- (2011) Michael Carnell et al. JOURNAL OF CELL BIOLOGY
- The Arp2/3 activator WASH regulates 5 1-integrin-mediated invasive migration
- (2011) T. Zech et al. JOURNAL OF CELL SCIENCE
- A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion
- (2011) Martin Harterink et al. NATURE CELL BIOLOGY
- SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
- (2011) Paul Temkin et al. NATURE CELL BIOLOGY
- VPS29 Is Not an Active Metallo-Phosphatase but Is a Rigid Scaffold Required for Retromer Interaction with Accessory Proteins
- (2011) James D. Swarbrick et al. PLoS One
- Sequence-Dependent Sorting of Recycling Proteins by Actin-Stabilized Endosomal Microdomains
- (2010) Manojkumar A. Puthenveedu et al. CELL
- New mechanisms and functions of actin nucleation
- (2010) Elif Nur Firat-Karalar et al. CURRENT OPINION IN CELL BIOLOGY
- The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics
- (2010) M. E. Harbour et al. JOURNAL OF CELL SCIENCE
- WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes
- (2010) D. Jia et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Assembly and Solution Structure of the Core Retromer Protein Complex
- (2010) Suzanne J. Norwood et al. TRAFFIC
- WASH, WHAMM and JMY: regulation of Arp2/3 complex and beyond
- (2010) Klemens Rottner et al. TRENDS IN CELL BIOLOGY
- The Arp2/3 Activator WASH Controls the Fission of Endosomes through a Large Multiprotein Complex
- (2009) Emmanuel Derivery et al. DEVELOPMENTAL CELL
- A FAM21-Containing WASH Complex Regulates Retromer-Dependent Sorting
- (2009) Timothy S. Gomez et al. DEVELOPMENTAL CELL
- Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
- (2009) M. N. J. Seaman et al. JOURNAL OF CELL SCIENCE
- The Wave complex is intrinsically inactive
- (2009) Emmanuel Derivery et al. CELL MOTILITY AND THE CYTOSKELETON
- Retromer
- (2008) Juan S Bonifacino et al. CURRENT OPINION IN CELL BIOLOGY
- The Structure and Function of the Retromer Protein Complex
- (2008) Brett M. Collins TRAFFIC
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started