Retromer-mediated endosomal protein sorting: All WASHed up!

Matthew N.J. Seaman; Alexis Gautreau; Daniel D. Billadeau

doi:10.1016/j.tcb.2013.04.010

Retromer-mediated endosomal protein sorting: All WASHed up!

Matthew N.J. Seaman, Alexis Gautreau, Daniel D. Billadeau

Oncology

Research output: Contribution to journal › Review article › peer-review

133 Scopus citations

Abstract

Endosomal protein sorting governs the fate of many physiologically important proteins involved in a panoply of cellular functions. Recent discoveries have revealed a vital role for endosomally localised branched actin patches in facilitating protein sorting. The formation of the actin patches has been shown to require the function of the WASH complex - the major endosomal actin polymerisation-promoting complex - which stimulates the activity of the ubiquitously expressed Arp2/3 complex. Another key component of the endosomal protein-sorting machinery is the retromer complex. Studies now show that retromer mediates the recruitment of the WASH complex and its regulators to endosomes. In this review, recent progress in understanding the role of the WASH complex along with retromer in endosomal protein sorting is discussed.

Original language	English (US)
Pages (from-to)	522-528
Number of pages	7
Journal	Trends in Cell Biology
Volume	23
Issue number	11
DOIs	https://doi.org/10.1016/j.tcb.2013.04.010
State	Published - Nov 2013

Keywords

Actin
Endosome
Fam21
Retromer
Sorting
WASH complex

ASJC Scopus subject areas

Cell Biology

Access to Document

10.1016/j.tcb.2013.04.010

Cite this

@article{442555654f524e4f85dca0d57a7c5d82,

title = "Retromer-mediated endosomal protein sorting: All WASHed up!",

abstract = "Endosomal protein sorting governs the fate of many physiologically important proteins involved in a panoply of cellular functions. Recent discoveries have revealed a vital role for endosomally localised branched actin patches in facilitating protein sorting. The formation of the actin patches has been shown to require the function of the WASH complex - the major endosomal actin polymerisation-promoting complex - which stimulates the activity of the ubiquitously expressed Arp2/3 complex. Another key component of the endosomal protein-sorting machinery is the retromer complex. Studies now show that retromer mediates the recruitment of the WASH complex and its regulators to endosomes. In this review, recent progress in understanding the role of the WASH complex along with retromer in endosomal protein sorting is discussed.",

keywords = "Actin, Endosome, Fam21, Retromer, Sorting, WASH complex",

author = "Seaman, {Matthew N.J.} and Alexis Gautreau and Billadeau, {Daniel D.}",

note = "Funding Information: M.N.J.S. is supported by a Senior Research Fellowship from the MRC (G0701444). Work on this topic in the Gautreau laboratory is funded by ANR (ANR-11 BSV2 014 01). D.D.B. is supported by the Mayo Foundation and NIH grant AI065474.",

year = "2013",

month = nov,

doi = "10.1016/j.tcb.2013.04.010",

language = "English (US)",

volume = "23",

pages = "522--528",

journal = "Trends in Cell Biology",

issn = "0962-8924",

publisher = "Elsevier Limited",

number = "11",

}

TY - JOUR

T1 - Retromer-mediated endosomal protein sorting

T2 - All WASHed up!

AU - Seaman, Matthew N.J.

AU - Gautreau, Alexis

AU - Billadeau, Daniel D.

N1 - Funding Information: M.N.J.S. is supported by a Senior Research Fellowship from the MRC (G0701444). Work on this topic in the Gautreau laboratory is funded by ANR (ANR-11 BSV2 014 01). D.D.B. is supported by the Mayo Foundation and NIH grant AI065474.

PY - 2013/11

Y1 - 2013/11

N2 - Endosomal protein sorting governs the fate of many physiologically important proteins involved in a panoply of cellular functions. Recent discoveries have revealed a vital role for endosomally localised branched actin patches in facilitating protein sorting. The formation of the actin patches has been shown to require the function of the WASH complex - the major endosomal actin polymerisation-promoting complex - which stimulates the activity of the ubiquitously expressed Arp2/3 complex. Another key component of the endosomal protein-sorting machinery is the retromer complex. Studies now show that retromer mediates the recruitment of the WASH complex and its regulators to endosomes. In this review, recent progress in understanding the role of the WASH complex along with retromer in endosomal protein sorting is discussed.

AB - Endosomal protein sorting governs the fate of many physiologically important proteins involved in a panoply of cellular functions. Recent discoveries have revealed a vital role for endosomally localised branched actin patches in facilitating protein sorting. The formation of the actin patches has been shown to require the function of the WASH complex - the major endosomal actin polymerisation-promoting complex - which stimulates the activity of the ubiquitously expressed Arp2/3 complex. Another key component of the endosomal protein-sorting machinery is the retromer complex. Studies now show that retromer mediates the recruitment of the WASH complex and its regulators to endosomes. In this review, recent progress in understanding the role of the WASH complex along with retromer in endosomal protein sorting is discussed.

KW - Actin

KW - Endosome

KW - Fam21

KW - Retromer

KW - Sorting

KW - WASH complex

UR - http://www.scopus.com/inward/record.url?scp=84886749671&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84886749671&partnerID=8YFLogxK

U2 - 10.1016/j.tcb.2013.04.010

DO - 10.1016/j.tcb.2013.04.010

M3 - Review article

C2 - 23721880

AN - SCOPUS:84886749671

SN - 0962-8924

VL - 23

SP - 522

EP - 528

JO - Trends in Cell Biology

JF - Trends in Cell Biology

IS - 11

ER -

Retromer-mediated endosomal protein sorting: All WASHed up!

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this