2021年4月1日 · RIAM belongs to the Mig-10/RIAM/Lamellipodin (MRL) family of adaptor proteins that share a similar structural module consisting of a Ras-association (RA) domain and a pleckstrin homology (PH) domain, also known as RA-PH. RIAM participates in the regulation of actin dynamics, cell adhesion, and cell migration (Lafuente et al., 2004).

2021年4月1日 · Cho et al. discovered that phosphorylation of RIAM by Src disrupts a common interaction that mediates RIAM oligomerization and promotes RIAM translocation to the plasma membrane. These findings elucidate a new regulatory …

RIAM has been shown to regulate the activation of VLA-4 and LFA-1 [21,22], the two integrins that play important roles in leukocyte trafficking during immune response [23,24]. RIAM has also been shown to regulate actin dynamics in T cells through Enabled/Vasodilator-stimulated phosphoprotein (Ena/VASP) family proteins and profilin .

2022年4月1日 · The Rap1/RIAM pathway is involved in signal integration for activation, actin remodeling and cytoskeletal reorganization in T cells, as well as in myeloid cell differentiation and function. RIAM is instrumental for phagocytosis, a process requiring particle recognition, cytoskeletal remodeling and membrane protrusion for engulfment and digestion.

Rap1-interacting molecule (RIAM) is a multidomain protein that regulates multiple functions in immune cells. RIAM contains an RA (RalGDS/AF-6 or Ras-association) domain, a PH (pleckstrin homology) domain, and two proline-rich regions. It also contains two putative coiled-coil regions at the amino (N) terminus.

2003年12月11日 · We have identified RIAM as a Rap1-GTP-interacting adaptor molecule. RIAM defines a family of adaptor molecules that contain a RA-like (Ras association) domain, a PH (pleckstrin homology) domain, and various proline-rich motifs. RIAM also interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics.

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2021年4月1日 · RIAM adopts an autoinhibitory configuration through an intramolecular interaction between the inhibitory (IN) segment and the Rap1-binding site on the RA domain. Two RIAM molecules are also packed together through the PH domain intermolecular interaction masking the phosphoinositide-binding site.

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