7d2h
From Proteopedia
Tetrameric coiled-coil structure of liprin-alpha2_H2
Structural highlights
FunctionLIPA2_HUMAN Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.[1] Publication Abstract from PubMedSynaptic scaffold proteins (e.g., liprin-alpha, ELKS, RIM, and RIM-BP) orchestrate ion channels, receptors, and enzymes at presynaptic terminals to form active zones for neurotransmitter release. The underlying mechanism of the active zone assembly remains elusive. Here, we report that liprin-alpha proteins have the potential to oligomerize through the N-terminal coiled-coil region. Our structural and biochemical characterizations reveal that a gain-of-function mutation promotes the self-assembly of the coiled coils in liprin-alpha2 by disrupting intramolecular interactions and promoting intermolecular interactions. By enabling multivalent interactions with ELKS proteins, the oligomerized coiled-coil region of liprin-alpha2 enhances the phase separation of the ELKS N-terminal segment. We further show that liprin-alpha2, by regulating the interplay between two phase separations of ELKS and RIM/RIM-BP, controls the protein distributions. These results imply that the complicated protein-protein interactions allow liprin-alpha to function with the active zone scaffolds and compartmentalize protein assemblies to achieve comprehensive functions in the active zone. Oligomerized liprin-alpha promotes phase separation of ELKS for compartmentalization of presynaptic active zone proteins.,Liang M, Jin G, Xie X, Zhang W, Li K, Niu F, Yu C, Wei Z Cell Rep. 2021 Mar 23;34(12):108901. doi: 10.1016/j.celrep.2021.108901. PMID:33761347[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
