JBC INTERFERin siRNA transfection reagent

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Papers In Press, published online ahead of print April 30, 2002
J. Biol. Chem, 10.1074/jbc.M111683200
Submitted on December 7, 2001
Revised on March 15, 2002
Accepted on April 26, 2002

Striatal enriched phosphatase 61 (STEP61) dephosphorylates Fyn at phosphotyrosine 420

Tri-Hung Nguyen, Jian Liu, and Paul J. Lombroso

Proteomics and Discovery, LumiCyte, Inc., Fremont, CA 94538

Corresponding Author: tnguyen{at}lumicyte.com

A family of protein tyrosine phosphatases enriched within the CNS called STEP has been implicated in the regulation of the NMDA (N-methyl-D-aspartate) receptor. STEP61, a membrane-associated isoform located in the postsynaptic densities (PSDs) of striatal neurons, contains two transmembrane domains, two proline-rich domains, and a kinase interacting motif (KIM). This study demonstrates that STEP61 associates with Fyn, a member of the Src family kinases that is also enriched in PSDs. By using HEK293 cells for co-transfection, we determined that a substrate trapping variant (STEP61 CS) binds to Fyn but not to other members of the Src family present in PSDs. In a complementary experiment, myc-tagged Fyn immunoprecipitates STEP61 CS. STEP61 binds to Fyn through one of its proline rich and the KIM domain, while Fyn binds to STEP61 through its SH2 and the unique N-terminal domain. STEP61 CS pulls down Fyn when the tyr420 site is phosphorylated. In vitro, wild-type STEP61 dephosphorylates Fyn at tyr420 but not at tyr531. These results suggest that STEP regulates the activity of Fyn by specifically dephosphorylating the regulatory tyr420 and may be one mechanism by which Fyn activity is decreased within PSDs.


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