Phosphoinositides play a fundamental role in clathrin-coat assembly at the cell surface. Several endocytic components and accessory factors contain independently folded phosphoinositide-binding modules that facilitate, in part, membrane placement at the bud site. As the clathrin-coat assembly process progresses toward deeply invaginated buds, focally synthesized phosphoinositides are dephosphorylated, principally through the action of the phosphoinositide polyphosphatase synaptojanin 1. Failure to catabolize polyphosphoinositides retards the fission process and endocytic activity. The long-splice isoform of synaptojanin 1, termed SJ170, contains a carboxyl-terminal extension that harbors interaction motifs for engaging several components of the endocytic machinery. Here, we demonstrate that in addition to DPF and FXDXF sequences, the SJ170 carboxyl terminus contains a novel AP-2 binding sequence, the WXXF motif. The WXXF sequence engages the independently folded a-subunit appendage th
|Journal||Journal of Biological Chemistry|
|State||Published - 2004|
Jha, A., Agostinelli, N. R., Mishra, S. K., Keyel, P., Hawryluk, M. J., & Traub, L. M. (2004). A Novel AP-2 Adaptor Interaction Motif Initially Identified in the Long-splice Isoform of Synaptojanin 1, SJ170. Journal of Biological Chemistry, 2281-2290.