| Primary Identifier | IPR045268 | Type | Family |
| Short Name | LIMA-like |
| description | This entry represents a group of LIM domain containing proteins, among which some proteins have been shown to bind actin, such as LIMA1/MICAL1/MICAL3 from humans. LIM domain and actin-binding protein 1 (LIMA1, also know as EPLIN) is a cytoskeleton-associated protein that regulates actin dynamics by cross-linking and stabilising filaments []. It was first identified as the product of a gene that is transcriptionally down-regulated or lost in a number of human epithelial tumor cells [, ]. In humans, there are two EPLIN isoforms, EPLIN alpha and EPLIN beta, both have a centrally located LIM domain that may mediate self-dimerisation. EPLIN inhibits Arp2/3 complex-mediated branching nucleation of actin filaments and stabilises actin filament networks []. EPLIN can be regulated through phophoryltion by extracellular signal-regulated kinase (ERK) [].MICAL (molecule Interacting with CasL) family is a group of multifunctional proteins that contain the calponin homology (CH), a LIM and a coiled-coil (CC) domains []. They interact with receptors on the target cells, help recruiting other proteins, and promote the modulation of their activity with respect to the downstream events []. There is only one MICAL protein found in Drosophila [], while there are 5 MICAL (MICAL1/2/3, MICAL-like1/2) isoforms found in vertebrates []. Drosophila MICAL and vertebrate MICAL1/2/3 contain an extra N-terminal FAD (flavin adenine dinucleotide binding monooxygenase) domain, whose structure resembles that of a flavo-enzyme, p-hydroxybenzoate hydroxylase []. Drosophila MICAL has an NADPH-dependent actin depolymerising activity []. Vertebrate MICALs are also shown to be effectors of small Rab GTPases, which play important roles in vesicular trafficking []. MICALs play roles in neural development and plasticity []. |
