Capping protein regulator and myosin 1 linker 3 (CARMIL3)

Capping protein regulator and myosin 1 linker 3 (CARMIL3) is one of three conserved vertebrate CARMIL family proteins that serve as multidomain regulators of the actin cytoskeleton[2]. CARMIL3 contains characteristic structural domains including a pleckstrin-homology (PH) domain, leucine-rich repeat (LRR) domain, helical dimerization domain, and C-terminal intrinsically disordered region with motifs for binding capping protein (CP) and class I myosin[2]. It binds the actin filament barbed end-capping protein directly and inhibits — but does not abolish — its capping activity, thereby promoting dynamics of filament elongation and turnover[2]. Cellular functions of CARMIL3 include regulation of actin assembly, enhancement of tumor cell migration and invasion, and control of synapse maturation in neurons[1][2]. CARMIL3 is primarily expressed in neurons and is upregulated in response to ischemic and oxidative neuronal injury, with emerging evidence that it may serve as a biomarker for neuronal stress or damage, such as after stroke[1]. Unlike many traditional drug targets, there are currently no drugs or therapies directly targeting CARMIL3, and its principal actions are as an intracellular scaffold and actin regulator rather than as an enzyme, receptor, ion channel, or other classic drug-binding protein[2][1].

Other names

Capping protein, Arp2/3 and myosin-I linker protein 3C14orf121LRRC16BBC008134crml-1Leucine-rich repeat-containing protein 16Bcapping protein regulator and myosin 1 linker protein 3