The 93 kDa protein gephyrin and tubulin associated with the inhibitory glycine receptor are phosphorylated by an endogenous protein kinase

Dieter Langosch, Werner Hoch, Heinrich Betz

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

The 93 kDa protein gephyrin is a tubulin binding peripheral membrane protein that is associated with the inhibitory glycine receptor and has been implicated in its anchoring at central synapses. Here, we demonstrate that gephyrin as well as co-purifying tubulin are phosphorylated by a kinase activity which is endogenous to highly purified glycine receptor preparations. This kinase phosphorylates serine and threonine residues and utilizes ATP, but not GTP, as phosphate donor. Its activity is not affected by various activators and/or inhibitors of cyclic nucleotide-dependent kinases, calcium/calmodulin-dependent kinases, or protein kinase C. A five-fold stimulation of kinase activity was, however, observed in the presence of poly-lysine. Phosphorylation of gephyrin and/or tubulin might regulate receptor/cytoskeleton interactions at postsynaptic membrane specializations.

Original languageEnglish
Pages (from-to)113-117
Number of pages5
JournalFEBS Letters
Volume298
Issue number2-3
DOIs
StatePublished - 24 Feb 1992
Externally publishedYes

Keywords

  • Glycine receptor
  • Protein phosphorylation
  • Tubulin

Fingerprint

Dive into the research topics of 'The 93 kDa protein gephyrin and tubulin associated with the inhibitory glycine receptor are phosphorylated by an endogenous protein kinase'. Together they form a unique fingerprint.

Cite this