Description: Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 2 (ATP2B2), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2), altering the location of this Ca2+ pump. Despite the similarity in C-terminal between the 'b' splice variants of Plasma membrane calcium-transporting ATPase 4 (ATP2B4) (-ETSV) and Plasma membrane calcium-transporting ATPase 2 (ATP2B2) (-ETSL), 'b' splice variants of ATP2B4 did not interact with either of the NHERFs whereas PMCA2b selectively preferred Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2) over Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). NHERFs have been previously implicated in the targeting, retention and regulation of membrane proteins including the β2-adrenergic receptor, cystic fibrosis transmembrane conductance regulator, and Trp4 Ca2+channel. This study suggests Plasma membrane calcium-transporting ATPase 2 (ATP2B2) may be under similar regulation.
Participants: (1) Plasma membrane calcium-transporting ATPase 2 (ATP2B2) (2) Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2)
(1) Plasma membrane Ca2+ ATPase isoform 2b interacts preferentially with Na+/H+ exchanger regulatory factor 2 in apical plasma membranes.DeMarco et al. J. Biol. Chem. (2002) (2) Apical scaffolding protein NHERF2 modulates the localization of alternatively spliced plasma membrane Ca2+ pump 2B variants in polarized epithelial cells.Padányi et al. J. Biol. Chem. (2010)
Other switches involving interfacesPDZ domain (Also known as DHR or GLGF) - 45 more (view)LIG_PDZ_Class_1 - 41 more (view)
