PAG1 directs SRC-family kinase intracellular localization to mediate receptor tyrosine kinase-induced differentiation.


Journal

Molecular biology of the cell
ISSN: 1939-4586
Titre abrégé: Mol Biol Cell
Pays: United States
ID NLM: 9201390

Informations de publication

Date de publication:
15 09 2020
Historique:
pubmed: 30 7 2020
medline: 23 6 2021
entrez: 30 7 2020
Statut: ppublish

Résumé

All receptor tyrosine kinases (RTKs) activate similar downstream signaling pathways through a common set of effectors, yet it is not fully understood how different receptors elicit distinct cellular responses to cause cell proliferation, differentiation, or other cell fates. We tested the hypothesis that regulation of SRC family kinase (SFK) signaling by the scaffold protein, PAG1, influences cell fate decisions following RTK activation. We generated a neuroblastoma cell line expressing a PAG1 fragment that lacks the membrane-spanning domain (PAG1

Identifiants

pubmed: 32726167
doi: 10.1091/mbc.E20-02-0135
pmc: PMC7550700
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
Membrane Proteins 0
PAG1 protein, human 0
Receptor Protein-Tyrosine Kinases EC 2.7.10.1
Proto-Oncogene Proteins c-fyn EC 2.7.10.2
src-Family Kinases EC 2.7.10.2

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

2269-2282

Subventions

Organisme : NIDCR NIH HHS
ID : R15 DE028434
Pays : United States
Organisme : NCRR NIH HHS
ID : P20 RR015583
Pays : United States
Organisme : NINDS NIH HHS
ID : R15 NS061303
Pays : United States
Organisme : NIGMS NIH HHS
ID : P20 GM103546
Pays : United States
Organisme : NINDS NIH HHS
ID : R15 NS070746
Pays : United States

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Auteurs

Lauren Foltz (L)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

Juan Palacios-Moreno (J)

University of Minnesota Medical School, Duluth, MN 55812.

Makenzie Mayfield (M)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

Shelby Kinch (S)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

Jordan Dillon (J)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

Jed Syrenne (J)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

Tyler Levy (T)

Cell Signaling Technology, Danvers, MA 01923.

Mark Grimes (M)

Division of Biological Sciences, Center for Biomolecular Structure and Dynamics, and Center for Structural and Functional Neuroscience, University of Montana, Missoula, MT 59812.

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Classifications MeSH