Capping protein regulator and myosin 1 linker 1 (CARMIL1)

CARMIL1 is a large multidomain protein that acts as a key regulator of actin filament dynamics at the plasma membrane, primarily by modulating the activity of heterodimeric capping protein (CP) at the barbed ends of actin filaments[1][3][5]. It binds directly to CP through the tandem CP-interaction (CPI) and CARMIL-specific interaction (CSI) motifs, inducing allosteric changes that decrease—but do not eliminate—CP’s actin-capping function[1][3]. This uncapping activity enhances actin polymerization and is vital for the formation and function of cellular projections such as lamellipodia and ruffles, as well as the process of macropinocytosis and cell migration[1][2][5]. CARMIL1 also interacts with myosin 1E/1F, Trio (a dual GEF), and various adaptors involved in signal transduction and membrane association[1][3]. It serves as a hub for cytoskeletal regulation and integrates signals for cell movement and shape changes[1][3]. Disease associations include gout and olecranon bursitis, and its dysfunction in cells leads to motility and signaling abnormalities[5][1]. There are currently no drugs or biomarker applications targeting CARMIL1, nor direct safety considerations related to therapeutic targeting[5][1][2][3].

Other names

F-actin-uncapping protein LRRC16ALRRC16ALRRC16dJ501N12.1FLJ20048dJ501N12.5CARMIL homologCARMILCARMIL1aCapping protein, Arp2/3 and myosin-I linker homolog 1/protein 1Leucine-rich repeat-containing protein 16ATesticular tissue protein Li 107