FEATURES

DESCRIPTION

Also known as PDLI4_RAT, Pdlim4, Ril. Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle (By similarity). Involved in reorganization of the actin cytoskeleton. In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers (PubMed:14729062, PubMed:22659164). Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1-containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (PubMed:15456832). Homodimer (By similarity). Interacts (via C-terminus only or via combined C-terminus and LIM domain, but not LIM domain only) with PTPN13 (via the second or fourth PDZ domains). Found in a complex with PTPN13 and TRIP6 (By similarity). Interacts (via PDZ domain) with ACTN1 and ACTN2 (via C-terminal SDL residues) (PubMed:14729062, PubMed:15456832). Interacts (via PDZ domain) with TRIP6 (via the second LIM domain or via the third LIM domain plus C-terminus) (By similarity). Interacts (via LIM domain) with GRIA1 (via C-terminus); this interaction as well as the interaction with alpha-actinin is required for their colocalization in early endosomes (PubMed:15456832). Interacts with PDLIM1 (PubMed:22659164). Forms (via LIM domain) a heterodimer with PDLIM3 (By similarity). Interacts directly with SRC (via kinase domain and to a lesser extent the SH2 domain) (By similarity).

EXTERNAL LINKS

Pdlim4

PDZ and LIM domain protein 4

Pdlim4

Molecular Synopsis