The Arp2/3 protein complex has been implicated in the control of actin polymerisation. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20 ...
The Arp2/3 protein complex has been implicated in the control of actin polymerisation. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. The precise function of p16-Arc is currently unknown. Its structure consists of a single domain containing a bundle of seven alpha helices [1,2].
This is the conserved leucine-rich domain (LRD) within the C-terminal domain of SPIN90 (also known as NCK interacting protein with SH3 domain (NCKIPSD)) from animals, Ldb17 from budding yeasts and Dip1 from fission yeasts [1]. Ldb17 is involved in th ...
This is the conserved leucine-rich domain (LRD) within the C-terminal domain of SPIN90 (also known as NCK interacting protein with SH3 domain (NCKIPSD)) from animals, Ldb17 from budding yeasts and Dip1 from fission yeasts [1]. Ldb17 is involved in the regulation of endocytosis in yeast [2]. SPIN90 is an F-actin binding protein that regulates actin polymerization and endocytosis [3]. It associates with and activates the Arp2/3 complex, without requiring a preformed actin filament [2,4,5]. This LRD, within the C-terminal armadillo repeat (ARM) domain of SPIN90, is important for activation of Arp2/3 complex [1].