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
Neuronjournal_title
Neuronauthors
Zhou Y,Schopperle WM,Murrey H,Jaramillo A,Dagan D,Griffith LC,Levitan IBdoi
10.1016/s0896-6273(00)80739-4subject
Has Abstractpub_date
1999-04-01 00:00:00pages
809-18issue
4eissn
0896-6273issn
1097-4199pii
S0896-6273(00)80739-4journal_volume
22pub_type
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