Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling

Baihao Su; Jinhua Wu

doi:10.33696/signaling.2.041

Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling

Baihao Su, Jinhua Wu

Fox Chase Cancer Center

Research output: Contribution to journal › Article › peer-review

Abstract

Integrins are cellular receptors that regulate cell adhesion and many other cellular functions. Integrins can be activated via an "inside-out pathway" that is promoted by RAP1 GTPase. RAP1-GTP-Interacting Adaptor Molecular (RIAM) mediates integrin activation by linking RAP1 GTPase to talin, an integrin activator. RIAM's function in integrin signaling is tightly regulated. In this commentary, we review recent studies of the molecular mechanisms underlying RIAM autoinhibition via both intramolecular interaction and oligomer assembly, and the phosphorylation-dependent activation of RIAM.

Original language	English
Pages (from-to)	103-110
Number of pages	8
Journal	Journal of cellular signaling
Volume	2
Issue number	2
DOIs	https://doi.org/10.33696/signaling.2.041
State	Published - 2021

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10.33696/signaling.2.041

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8813058/

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title = "Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling",

abstract = "Integrins are cellular receptors that regulate cell adhesion and many other cellular functions. Integrins can be activated via an {"}inside-out pathway{"} that is promoted by RAP1 GTPase. RAP1-GTP-Interacting Adaptor Molecular (RIAM) mediates integrin activation by linking RAP1 GTPase to talin, an integrin activator. RIAM's function in integrin signaling is tightly regulated. In this commentary, we review recent studies of the molecular mechanisms underlying RIAM autoinhibition via both intramolecular interaction and oligomer assembly, and the phosphorylation-dependent activation of RIAM.",

author = "Baihao Su and Jinhua Wu",

year = "2021",

doi = "10.33696/signaling.2.041",

language = "English",

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pages = "103--110",

journal = "Journal of cellular signaling",

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AU - Wu, Jinhua

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AB - Integrins are cellular receptors that regulate cell adhesion and many other cellular functions. Integrins can be activated via an "inside-out pathway" that is promoted by RAP1 GTPase. RAP1-GTP-Interacting Adaptor Molecular (RIAM) mediates integrin activation by linking RAP1 GTPase to talin, an integrin activator. RIAM's function in integrin signaling is tightly regulated. In this commentary, we review recent studies of the molecular mechanisms underlying RIAM autoinhibition via both intramolecular interaction and oligomer assembly, and the phosphorylation-dependent activation of RIAM.

UR - https://pubmed.ncbi.nlm.nih.gov/35128538/

U2 - 10.33696/signaling.2.041

DO - 10.33696/signaling.2.041

M3 - Article

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SN - 2692-0638

VL - 2

SP - 103

EP - 110

JO - Journal of cellular signaling

JF - Journal of cellular signaling

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ER -

Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling

Abstract

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