CD2 cytoplasmic tail binding protein 2 (CD2BP2)

CD2 cytoplasmic tail binding protein 2 (CD2BP2) is a bi-functional adaptor protein characterized by the presence of a highly conserved GYF domain, which enables specific protein–protein interactions[1][2][3][5]. In the cytoplasm of T cells, CD2BP2 binds proline-rich motifs in the cytoplasmic tail of the CD2 surface antigen, but its contribution to T cell receptor signaling is likely minimal, as knockdown does not significantly affect cytokine production[1][4][5]. The predominant and essential role of CD2BP2 occurs in the nucleus, where it functions as a component of the U5 small nuclear ribonucleoprotein (snRNP) complex, a core building block of the spliceosome[1][2][3]. Here, CD2BP2 is required for proper assembly, maturation, and recycling of the U5 snRNP and is essential for splicing of pre-mRNA, with its loss leading to global defects in splicing, exon skipping, and changes in cell proliferation and apoptosis[2][3]. CD2BP2 is also implicated in the regulation of the microRNA-induced silencing complex and maintenance of microRNA levels, highlighting its role in post-transcriptional gene regulation[1]. Genetic knockout of CD2BP2 results in embryonic lethality in mice, pointing to its critical cellular function[3]. There is currently no direct evidence that CD2BP2 is a therapeutic target or that it is modulated by any approved drugs.

Other names

CD2 antigen cytoplasmic tail-binding protein 2KIAA1178CD2 cytoplasmic domain-binding protein 2CD2 tail-binding protein 2U5-52KLIN1Snu40PPP1R59protein phosphatase 1 regulatory subunit 59FWP010