What question did this study set out to answer?

To determine whether cAMP-dependent and endogenous protein kinases phosphorylate and regulate the function of dendrotoxin-binding potassium channels.

July 25, 1989Biochemistry

Dendrotoxin-binding brain membrane protein displays a potassium channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations

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Authors

HRHubert RehmKrankenhaus vom Roten Kreuz SPSiegried PelzerDalhousie University CCClaude CochetInserm

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Implication

In vitro study demonstrates that kinase phosphorylation stimulates dendrotoxin-binding potassium channels in brain membranes, suggesting enzymatic control of neuronal excitability.

Key Points

To determine whether cAMP-dependent and endogenous protein kinases phosphorylate and regulate the function of dendrotoxin-binding potassium channels.
Purified dendrotoxin I- and mast cell degranulating peptide-binding membrane protein complexes from brain tissue.
Assayed phosphorylation using cAMP-dependent protein kinase and an endogenous membrane protein kinase.
Reconstituted the purified protein to assess potassium channel activity following phosphorylation.
Both cAMP-dependent protein kinase and an endogenous kinase phosphorylated the 76–80 kDa toxin-binding subunit.
Phosphorylation by either kinase stimulated the functional channel activity of the reconstituted dendrotoxin-sensitive potassium channel.

Cite This Study

Rehm et al. (1989) studied this question.

synapsesocial.com/papers/6a7e1403fc4f0e65bd3bfa85 https://doi.org/10.1021/bi00441a044

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Implication

In vitro study demonstrates that kinase phosphorylation stimulates dendrotoxin-binding potassium channels in brain membranes, suggesting enzymatic control of neuronal excitability.

Dendrotoxin-binding brain membrane protein displays a potassium channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations

Discussion

Member takes

Implication

Key Points

Cite This Study

Dendrotoxin-binding brain membrane protein displays a potassium channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations

Discussion

Member takes

Implication

Key Points

Cite This Study

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