Casein kinase II phosphorylates the neural cell adhesion molecule L1

Eric V. Wong, Andrew W. Schaefer, Gary Landreth, Vance Lemmon

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

L1 is an axonal cell adhesion molecule found primarily on projection exons of both the CNS and PNS. It is a phosphorylated membrane-spanning glycoprotein that can be immunoprecipitated from rat brain membranes in association with protein kinase activities. Western blot analysis demonstrates that casein kinase II (CKII), a ubiquitous serine/threonine kinase enriched in brain, is present in these immunoprecipitates. CKII preparations partially purified from PC12 cells are able to phosphorylate recombinant L1 cytoplasmic domain (L1CD), which consists of residues 1,144- 1,257. Using these as well as more highly purified kinase preparations, phosphorylation assays of small peptides derived from the L1CD were performed. CKII was able to phosphorylate a peptide encompassing amino acids (aa) 1,173-1,185, as well as a related peptide representing an alternatively spliced nonneuronal L1 isoform that lacks aa 1,1771,180. Both peptides were phosphorylated with similar kinetic profiles. Serine to alanine substitutions in these peptides indicate that the CKII phosphorylation site is at Ser1,181. This is consistent with experiments in which L1CD was phosphorylated by these kinase preparations, digested, and the radiolabeled fragments sequenced. Furthermore, when L1 immunoprecipitates were used to phosphorylate L1CD, one of the residues phosphorylated is the same residue phosphorylated by CKII. Finally, in vivo radiolabeling indicates that Ser1,181 is phosphorylated in newborn rat brain. These data show that CKII is associated with and able to phosphorylate L1. This phosphorylation may be important in regulating certain aspects of L1 function, such as adhesivity or signal transduction.

Original languageEnglish
Pages (from-to)779-786
Number of pages8
JournalJournal of Neurochemistry
Volume66
Issue number2
StatePublished - Feb 1 1996
Externally publishedYes

Fingerprint

Neural Cell Adhesion Molecule L1
Casein Kinase II
Phosphorylation
Peptides
Brain
Rats
Phosphotransferases
Membranes
Amino Acids
Signal transduction
Protein-Serine-Threonine Kinases
PC12 Cells
Membrane Glycoproteins
Cell Adhesion Molecules
Alanine
Protein Kinases
Serine
Exons
Assays
Signal Transduction

Keywords

  • Casein kinase II
  • Cell adhesion molecule
  • L1 function
  • Phosphorylation
  • Rat brain
  • Serine/threonine kinase

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Casein kinase II phosphorylates the neural cell adhesion molecule L1. / Wong, Eric V.; Schaefer, Andrew W.; Landreth, Gary; Lemmon, Vance.

In: Journal of Neurochemistry, Vol. 66, No. 2, 01.02.1996, p. 779-786.

Research output: Contribution to journalArticle

Wong, EV, Schaefer, AW, Landreth, G & Lemmon, V 1996, 'Casein kinase II phosphorylates the neural cell adhesion molecule L1', Journal of Neurochemistry, vol. 66, no. 2, pp. 779-786.
Wong, Eric V. ; Schaefer, Andrew W. ; Landreth, Gary ; Lemmon, Vance. / Casein kinase II phosphorylates the neural cell adhesion molecule L1. In: Journal of Neurochemistry. 1996 ; Vol. 66, No. 2. pp. 779-786.
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