A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals.

Abstract:

:Slob is a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSlo) calcium-dependent potassium (K(Ca)) channel. A yeast two-hybrid screen with Slob as bait identifies the zeta isoform of 14-3-3 as a Slob-binding protein. Coimmunoprecipitation experiments from Drosophila heads and transfected cells confirm that 14-3-3 interacts with dSlo via Slob. All three proteins are colocalized presynaptically at Drosophila neuromuscular junctions. Two serine residues in Slob are required for 14-3-3 binding, and the binding is dynamically regulated in Drosophila by calcium/calmodulin-dependent kinase II (CaMKII) phosphorylation. 14-3-3 coexpression dramatically alters dSlo channel properties when wild-type Slob is present but not when a double serine mutant Slob that is incapable of binding 14-3-3 is present. The results provide evidence for a dSlo/Slob/14-3-3 regulatory protein complex.

journal_name

Neuron

journal_title

Neuron

authors

Zhou Y,Schopperle WM,Murrey H,Jaramillo A,Dagan D,Griffith LC,Levitan IB

doi

10.1016/s0896-6273(00)80739-4

subject

Has Abstract

pub_date

1999-04-01 00:00:00

pages

809-18

issue

4

eissn

0896-6273

issn

1097-4199

pii

S0896-6273(00)80739-4

journal_volume

22

pub_type

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