Lin-7 homolog C; Lin-7C; mammalian lin-seven protein 3; MALS-3; vertebrate lin-7 homolog 3; Veli-3 protein (LIN7C, MALS3, VELI3)
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Function
- role in establishing & maintaining asymmetric distribution of channels & receptors at the plasma membrane of polarized cells
- forms membrane-associated multiprotein complexes that may regulate delivery & recycling of proteins to correct membrane domains
- tripartite complex composed of LIN7C, CASK & APBA1 couple synaptic vesicle exocytosis to cell adhesion in brain (putative)
- ensures proper localization of GRIN2B (NMDA receptor subunit 2B) to neuronal postsynaptic density
- localizes synaptic vesicles at synapses where it is recruited by beta-catenin & cadherin
- required to localize Kir2 channels, GABA transporter (SLC6A12) & EGFR/ERBB1, ERBB2, ERBB3 & ERBB4 to the basolateral membrane of epithelial cells
- forms two exclusive ternary complexes with CASK & APBA1 or CASKIN1
- interacts with other modular proteins containing protein- protein interaction domains including MPP5, MPP6, DLG1, DLG2 & DLG3 through its L27 domain
- interacts with DLG4, GRIN2B, CDH1, CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 & probably KCNJ2/Kir2.1 & SLC6A12/BGT-1 via its PDZ domain
- Ca+-dependent association of LIN7A with cadherin & beta-catenin at synaptic junctions requires actin cytoskeleton
- interacts with EGFR, ERBB2, ERBB3 & ERBB4 with both PDZ & KID domains
- associates with KIF17 via APBA1.
Structure
- belongs to the lin-7 family
- contains 1 L27 domain, mediates interaction with CASK & is involved in formation of multimeric complexes & the association of LIN7 to membranes
- contains 1 PDZ domain (DHR domain), regulates endocytosis & recycling of receptor at cell membrane
- kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane
Compartment
- cell membrane, cell junction, synapse, postsynaptic membrane, postsynaptic density
- localized to postsynaptic densities of neurons & epithelial cell-cell junctions
- mainly basolateral in renal epithelial cells
Alternative splicing
named isoforms=1