Capping protein, Arp2/3 and myosin-I linker protein 2

Definition:

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. 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 and T regulatory cells.

References:

[1]. Yun Liang, et al. Distinct roles for CARMIL isoforms in cell migration. Mol Biol Cell. 2009 Dec;20(24):5290-305. [Content Brief]

[2]. T Schober, et al. A human immunodeficiency syndrome caused by mutations in CARMIL2. Nat Commun. 2017 Jan 23;8:14209. [Content Brief]

[3]. Yi Wang, et al. Dual T cell- and B cell-intrinsic deficiency in humans with biallelic RLTPR mutations. J Exp Med. 2016 Oct 17;213(11):2413-2435. [Content Brief]

[4]. M Hunter Lanier, et al. Cell Migration and Invadopodia Formation Require a Membrane-binding Domain of CARMIL2. J Biol Chem. 2016 Jan 15;291(3):1076-91. [Content Brief]

[5]. M Hunter Lanier, et al. CARMIL2 is a novel molecular connection between vimentin and actin essential for cell migration and invadopodia formation. Mol Biol Cell. 2015 Dec 15;26(25):4577-88. [Content Brief]

[6]. Romain Roncagalli, et al. The scaffolding function of the RLTPR protein explains its essential role for CD28 co-stimulation in mouse and human T cells. J Exp Med. 2016 Oct 17;213(11):2437-2457. [Content Brief]

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