Structural, biochemical, and functional properties of the Rap1-Interacting Adaptor Molecule (RIAM)

Biomed J. 2022 Apr;45(2):289-298. doi: 10.1016/j.bj.2021.09.005. Epub 2021 Oct 1.

Abstract

Leukocytes, the leading players of immune system, are involved in innate and adaptive immune responses. Leukocyte adhesion to endothelial cells during transmigration or to antigen presenting cells during T cell activation, requires integrin activation through a process termed inside-out integrin signaling. In hematopoietic cells, Rap1 and its downstream effector RIAM (Rap1-interacting adaptor molecule) form a cornerstone for inside-out integrin activation. 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. In the present review, we discuss the structural and molecular properties of RIAM and the recent discoveries regarding the functional role of the Rap1/RIAM module in hematopoietic cells.

Keywords: Adhesion; Integrins; Leukocytes; Phagocytosis; RIAM; Rap1.

Publication types

  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Adaptor Proteins, Signal Transducing / metabolism
  • Cell Adhesion
  • Endothelial Cells / metabolism
  • Humans
  • Integrins / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism

Substances

  • APBB1IP protein, human
  • Adaptor Proteins, Signal Transducing
  • Integrins
  • Membrane Proteins