| Primary Identifier | IPR028563 | Type | Family |
| Short Name | MICAL-L |
| description | 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 []. MICAL-like protein 1 (MICAL-L1) interacts with small G proteins and regulates endocytic recycling of receptors [, ]. It forms a complex with Rab13 that regulates EGFR trafficking at late endocytic pathways []. MICAL-L1 also forms a complex with Arf6 that regulates Rab8a function. MICAL-L1 can be regulated by Rab35 [].MICAL-like protein 2 (MICAL-L2, also known as JRAB) interacts with Rab13 []and Rab8 to regulate the endocytic recycling of occludin, claudin and E-cadherin to the plasma membrane. It may thereby regulate the establishment of tight junctions and adherens junctions []. MICAL-L2/JRAB also regulates the reorganisation of the actin cytoskeleton through interactions with actinin-1, actinin-4, and filamentous actin [], and via filamins during cell spreading []. |
