High impact information on Sh3gl2

• Endophilin I exhibits lysophosphatidic acid acyl transferase (LPAAT) activity, and endophilin-I-mediated SLMV formation requires the transfer of the unsaturated fatty acid arachidonate to lysophosphatidic acid, converting it to phosphatidic acid [1].
• These studies show that Arc/Arg3.1 regulates endophilin 3 and dynamin 2, two components of the endocytosis machinery [2].
• Consistent with this, immunofluorescence analysis of endophilin B1b transfected into fibroblasts shows an intracellular reticular staining, which in part overlaps with that of endogenous dynamin [3].
• The protein was named RICH-1 (RhoGAP interacting with CIP4 homologues), and, in addition to the RhoGAP domain, it contained an N-terminal domain with endophilin homology and a C-terminal proline-rich domain [4].
• The site of interaction was suggested to be the SH-3-binding domain of Mta1 and SH-3 domain of endophilin 3 [5].

Biological context of Sh3gl2

• Screening of a cDNA library prepared from mouse embryo yielded positive clones coding for endophilin 3 [5].
• This protection afforded by Alix mutants was abolished after deletion of the TSG101, but not of the endophilin, binding sites [6].

Anatomical context of Sh3gl2

• Endophilin has been implicated in the retrieval of membrane via endocytosis of clathrin-coated vesicles, which is crucial for the maintenance of neurotransmitter exocytosis during stimulation; both exocytosis and endocytosis are regulated by intracellular calcium levels [7].
• The Mta1 and endophilin 3 transcripts were highly expressed in testis and brain [5].

Other interactions of Sh3gl2

• The cytoplasmic domain comprises 103 amino acids containing proline-rich endophilin I, Src homology 3 (SH3), and phox homology domain-containing protein (SH3PX1) binding motifs [8].

References