RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.
allosteric regulation
cancer
cell signaling
crystal structure
protein phosphatase
protein structure
signal transduction
tyrosine-protein phosphatase (tyrosine phosphatase)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
10 04 2020
10 04 2020
Historique:
received:
25
11
2019
revised:
03
03
2020
pubmed:
7
3
2020
medline:
15
12
2020
entrez:
7
3
2020
Statut:
ppublish
Résumé
Receptor-type protein tyrosine phosphatase α (RPTPα) is an important positive regulator of SRC kinase activation and a known promoter of cancer growth, fibrosis, and arthritis. The domain structure of RPTPs comprises an extracellular region, a transmembrane helix, and two tandem intracellular catalytic domains referred to as D1 and D2. The D2 domain of RPTPs is believed to mostly play a regulatory function; however, no regulatory model has been established for RPTPα-D2 or other RPTP-D2 domains. Here, we solved the 1.8 Å resolution crystal structure of the cytoplasmic region of RPTPα, encompassing D1 and D2, trapped in a conformation that revealed a possible mechanism through which D2 can allosterically inhibit D1 activity. Using a D2-truncation RPTPα variant and mutational analysis of the D1/D2 interfaces, we show that D2 inhibits RPTPα phosphatase activity and identified a
Identifiants
pubmed: 32139509
pii: S0021-9258(17)48588-7
doi: 10.1074/jbc.RA119.011808
pmc: PMC7152759
doi:
Substances chimiques
PTPRA protein, human
EC 3.1.3.48
Protein Tyrosine Phosphatases
EC 3.1.3.48
Receptor-Like Protein Tyrosine Phosphatases, Class 4
EC 3.1.3.48
Banques de données
PDB
['1YFO', '1Y15', '2JJD', '2FH7', '3SR9', '4BPC']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4923-4936Subventions
Organisme : NIAMS NIH HHS
ID : R01 AR066053
Pays : United States
Organisme : NIH HHS
ID : S10 OD021832
Pays : United States
Informations de copyright
© 2020 Wen et al.
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