SCIN
Description
The SCIN (scinderin) is a protein-coding gene located on chromosome 7.
Scinderin (also known as adseverin) is a protein that in humans is encoded by the SCIN gene. Scinderin is an actin severing protein belonging to the gelsolin superfamily. It was discovered in Dr. Trifaro's laboratory at the University of Ottawa, Canada. Secretory tissues are rich in scinderin. In these tissues scinderin, a calcium dependent protein, regulates cortical actin networks. Normally secretory vesicles are excluded from release sites on the plasma membrane by the presence of a cortical actin filament network. During cell stimulation, calcium channels open allowing calcium ions to enter the secretory cell. Increase in intracellular calcium activates scinderin with the consequent actin filament severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.
Scinderin (also known as Adseverin) is a calcium-dependent actin filament-severing protein that plays a regulatory role in exocytosis by influencing the organization of the microfilament network beneath the plasma membrane. Its severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2). In vitro, it exhibits barbed end capping and nucleating activities in the presence of calcium. Scinderin is essential for megakaryocyte differentiation, maturation, polyploidization, and apoptosis, leading to the release of platelet-like particles. It also plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts. Furthermore, it regulates chondrocyte proliferation and differentiation. Scinderin inhibits cell proliferation and tumorigenesis, with signaling mediated by MAPK, p38, and JNK pathways.
SCIN is also known as -.
