PMID- 32528512
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20220202
IS  - 1664-462X (Print)
IS  - 1664-462X (Electronic)
IS  - 1664-462X (Linking)
VI  - 11
DP  - 2020
TI  - The Beginning of the End: Initial Steps in the Degradation of Plasma Membrane 
      Proteins.
PG  - 680
LID - 10.3389/fpls.2020.00680 [doi]
LID - 680
AB  - The plasma membrane (PM), as border between the inside and the outside of a cell, 
      is densely packed with proteins involved in the sensing and transmission of 
      internal and external stimuli, as well as transport processes and is therefore 
      vital for plant development as well as quick and accurate responses to the 
      environment. It is consequently not surprising that several regulatory pathways 
      participate in the tight regulation of the spatiotemporal control of PM proteins. 
      Ubiquitination of PM proteins plays a key role in directing their entry into the 
      endo-lysosomal system, serving as a signal for triggering endocytosis and further 
      sorting for degradation. Nevertheless, a uniting picture of the different roles 
      of the respective types of ubiquitination in the consecutive steps of 
      down-regulation of membrane proteins is still missing. The trans-Golgi network 
      (TGN), which acts as an early endosome (EE) in plants receives the endocytosed 
      cargo, and here the decision is made to either recycled back to the PM or further 
      delivered to the vacuole for degradation. A multi-complex machinery, the 
      endosomal sorting complex required for transport (ESCRT), concentrates 
      ubiquitinated proteins and ushers them into the intraluminal vesicles of 
      multi-vesicular bodies (MVBs). Several ESCRTs have ubiquitin binding subunits, 
      which anchor and guide the cargos through the endocytic degradation route. Basic 
      enzymes and the mode of action in the early degradation steps of PM proteins are 
      conserved in eukaryotes, yet many plant unique components exist, which are often 
      essential in this pathway. Thus, deciphering the initial steps in the degradation 
      of ubiquitinated PM proteins, which is the major focus of this review, will 
      greatly contribute to the larger question of how plants mange to fine-tune their 
      responses to their environment.
CI  - Copyright (c) 2020 Schwihla and Korbei.
FAU - Schwihla, Maximilian
AU  - Schwihla M
AD  - Department of Applied Genetics and Cell Biology, Institute of Molecular Plant 
      Biology, University of Natural Resources and Life Sciences, Vienna, Vienna, 
      Austria.
FAU - Korbei, Barbara
AU  - Korbei B
AD  - Department of Applied Genetics and Cell Biology, Institute of Molecular Plant 
      Biology, University of Natural Resources and Life Sciences, Vienna, Vienna, 
      Austria.
LA  - eng
GR  - P 30850/FWF_/Austrian Science Fund FWF/Austria
PT  - Journal Article
PT  - Review
DEP - 20200521
PL  - Switzerland
TA  - Front Plant Sci
JT  - Frontiers in plant science
JID - 101568200
PMC - PMC7253699
OTO - NOTNLM
OT  - CME
OT  - ESCRT (endosomal sorting complex required for transport)
OT  - degradation
OT  - plasma membrane protein
OT  - ubiquitin
EDAT- 2020/06/13 06:00
MHDA- 2020/06/13 06:01
PMCR- 2020/01/01
CRDT- 2020/06/13 06:00
PHST- 2020/02/28 00:00 [received]
PHST- 2020/04/30 00:00 [accepted]
PHST- 2020/06/13 06:00 [entrez]
PHST- 2020/06/13 06:00 [pubmed]
PHST- 2020/06/13 06:01 [medline]
PHST- 2020/01/01 00:00 [pmc-release]
AID - 10.3389/fpls.2020.00680 [doi]
PST - epublish
SO  - Front Plant Sci. 2020 May 21;11:680. doi: 10.3389/fpls.2020.00680. eCollection 
      2020.