PMID- 30190330
OWN - NLM
STAT- MEDLINE
DCOM- 20190307
LR  - 20220129
IS  - 1470-8752 (Electronic)
IS  - 0300-5127 (Print)
IS  - 0300-5127 (Linking)
VI  - 46
IP  - 5
DP  - 2018 Oct 19
TI  - Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs 
      in sorting activated epidermal growth factor receptor to the multivesicular body.
PG  - 1037-1046
LID - 10.1042/BST20170443 [doi]
AB  - Sorting of activated epidermal growth factor receptor (EGFR) into intraluminal 
      vesicles (ILVs) within the multivesicular body (MVB) is an essential step during 
      the down-regulation of the receptor. The machinery that drives EGFR sorting 
      attaches to the cytoplasmic face of the endosome and generates vesicles that bud 
      into the endosome lumen, but somehow escapes encapsulation itself. This machinery 
      is termed the ESCRT (endosomal sorting complexes required for transport) pathway, 
      a series of multi-protein complexes and accessory factors first identified in 
      yeast. Here, we review the yeast ESCRT pathway and describe the corresponding 
      components in mammalian cells that sort EGFR. One of these is His domain protein 
      tyrosine phosphatase (HD-PTP/PTPN23), and we review the interactions involving 
      HD-PTP and ESCRTs. Finally, we describe a working model for how this ESCRT 
      pathway might overcome the intrinsic topographical problem of EGFR sorting to the 
      MVB lumen.
CI  - (c) 2018 The Author(s).
FAU - Tabernero, Lydia
AU  - Tabernero L
AD  - School of Biological Sciences, Faculty of Biology Medicine and Health, University 
      of Manchester, Manchester Academic Health Science Centre, Manchester, U.K.
FAU - Woodman, Philip
AU  - Woodman P
AUID- ORCID: 0000-0001-9497-1235
AD  - School of Biological Sciences, Faculty of Biology Medicine and Health, University 
      of Manchester, Manchester Academic Health Science Centre, Manchester, U.K. 
      philip.woodman@manchester.ac.uk.
LA  - eng
GR  - G0001128/MRC_/Medical Research Council/United Kingdom
GR  - G0701140/MRC_/Medical Research Council/United Kingdom
GR  - BB/K008773/1/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - MR/K011049/1/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20180906
PL  - England
TA  - Biochem Soc Trans
JT  - Biochemical Society transactions
JID - 7506897
RN  - 0 (Endosomal Sorting Complexes Required for Transport)
RN  - 0 (Ligands)
RN  - EC 2.7.10.1 (EGFR protein, human)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 3.1.3.48 (PTPN23 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases, Non-Receptor)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cell Membrane/metabolism
MH  - Decision Making
MH  - Down-Regulation
MH  - Endosomal Sorting Complexes Required for Transport/*genetics
MH  - Endosomes/metabolism
MH  - ErbB Receptors/*metabolism
MH  - Humans
MH  - Ligands
MH  - Multivesicular Bodies
MH  - Protein Conformation
MH  - Protein Domains
MH  - Protein Multimerization
MH  - Protein Transport
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - Protein Tyrosine Phosphatases, Non-Receptor/*metabolism
MH  - Saccharomyces cerevisiae/*metabolism
PMC - PMC6195633
OTO - NOTNLM
OT  - ESCRT
OT  - HD-PTP
OT  - MVB
OT  - endosomal sorting
OT  - epidermal growth factor receptor
COIS- The Authors declare that there are no competing interests associated with the 
      manuscript.
EDAT- 2018/09/08 06:00
MHDA- 2019/03/08 06:00
PMCR- 2018/09/06
CRDT- 2018/09/08 06:00
PHST- 2018/04/03 00:00 [received]
PHST- 2018/05/31 00:00 [revised]
PHST- 2018/07/31 00:00 [accepted]
PHST- 2018/09/08 06:00 [pubmed]
PHST- 2019/03/08 06:00 [medline]
PHST- 2018/09/08 06:00 [entrez]
PHST- 2018/09/06 00:00 [pmc-release]
AID - BST20170443 [pii]
AID - BST-46-1037 [pii]
AID - 10.1042/BST20170443 [doi]
PST - ppublish
SO  - Biochem Soc Trans. 2018 Oct 19;46(5):1037-1046. doi: 10.1042/BST20170443. Epub 
      2018 Sep 6.