SWAP70 - Switch-associated protein 70S | Elisa - Clia - Antibody - Protein

Background

Switch-associated protein 70 (SWAP70) is a guanine nucleotide exchange factor (GEF) that plays a crucial role in cytoskeletal rearrangement and signal transduction. It was initially identified as a protein involved in the regulation of immunoglobulin class switching in B cells, but subsequent research has revealed its broader functions in various cellular processes. SWAP70 is implicated in the regulation of actin cytoskeleton dynamics, membrane ruffling, cell migration, and adhesion. It is expressed in various tissues and has significant roles in both immune and non-immune cells. SWAP70's activity is regulated by phosphoinositides and small GTPases, particularly the Rho family of GTPases.

Protein Structure

SWAP70 is characterized by several functional domains:

• PH (Pleckstrin Homology) Domain: This domain binds to phosphoinositides in the plasma membrane, anchoring SWAP70 to specific membrane sites.
• Rho-GEF Domain: Responsible for its activity as a guanine nucleotide exchange factor, facilitating the exchange of GDP for GTP on Rho GTPases.
• Coiled-Coil Domain: Involved in protein-protein interactions, contributing to the formation of multiprotein complexes.
• EF-Hand Motif: Typically associated with calcium binding, although its specific function in SWAP70 may vary.

Classification and Subtypes

SWAP70 belongs to the family of GEFs, which are classified based on their ability to activate small GTPases. There are no specific subtypes of SWAP70, but it is part of a broader group of proteins that regulate Rho GTPase signaling.

Function and Biological Significance

SWAP70 plays several vital roles in cellular processes:

• Actin Cytoskeleton Regulation: By activating Rho GTPases, SWAP70 regulates the actin cytoskeleton, influencing cell shape, migration, and adhesion.
• Cell Migration and Adhesion: Essential for directed cell movement and adhesion to the extracellular matrix, crucial for immune cell trafficking and tissue development.
• Membrane Ruffling: Involved in the formation of membrane ruffles, which are necessary for cell movement and endocytosis.
• B Cell Function: Initially discovered for its role in immunoglobulin class switching in B cells, impacting antibody diversity.
• Signal Transduction: Participates in various signaling pathways, modulating cellular responses to external stimuli.

Clinical Issues

Dysregulation or mutations in SWAP70 are associated with several diseases:

• Cancer: Abnormal expression or function of SWAP70 can contribute to cancer progression by affecting cell migration and invasion. It has been implicated in various cancers, including breast, colorectal, and pancreatic cancers.
• Autoimmune Diseases: Given its role in immune cell function, alterations in SWAP70 can influence autoimmune responses and are associated with diseases such as rheumatoid arthritis.
• Developmental Disorders: Proper function of SWAP70 is crucial for normal cellular development and tissue formation; disruptions can lead to developmental abnormalities.

Summary

Switch-associated protein 70 (SWAP70) is a guanine nucleotide exchange factor crucial for the regulation of actin cytoskeleton dynamics, cell migration, adhesion, and signal transduction. It comprises several functional domains, including the PH domain, Rho-GEF domain, coiled-coil domain, and EF-hand motif, which facilitate its diverse roles in cellular processes. SWAP70's involvement in immune cell function and cytoskeletal rearrangement makes it a key player in both normal cellular physiology and disease pathogenesis. Dysregulation of SWAP70 is linked to cancer progression, autoimmune diseases, and developmental disorders, highlighting its importance as a potential therapeutic target.