Carmil2
Domain
The N-terminal leucine-rich repeat (LRR) domain is necessary for localization to vimentin filaments. The C-terminus is necessary for localization to the cell membrane.
Function
Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization. Plays a role in cell protrusion formations; involved in cell polarity, lamellipodial assembly, membrane ruffling and macropinosome formations. Involved as well in cell migration and invadopodia formation during wound healing (By similarity). Required for CD28-mediated stimulation of NF-kappa-B signaling, involved in naive T cells activation, maturation into T memory cells, and differentiation into T helper cells (PubMed:27647348). Required for CD28-mediated differentiation of T regulatory cells (By similarity).
Sequence Similarities
Belongs to the CARMIL family.
Cellular localization
- Cytoplasm
- Cytoplasm
- Cytoskeleton
- Cell membrane
- Peripheral membrane protein
- Cytoplasmic side
- Cell projection
- Lamellipodium
- Cell projection
- Ruffle
- Colocalizes to dynamic vimentin filaments both in the central cytoplasm and at leading edges of migrating cells. Colocalizes with F-actin, Arp2/3 complex and cortactin to leading edge lamellipodia, ruffles and macropinosomes of migrating cells.
Alternative names
Lrrc16c, Rltpr, Carmil2, Capping protein regulator and myosin 1 linker 2, F-actin-uncapping protein RLTPR, Leucine-rich repeat-containing protein 16C