Literature DB >> 8981445

The neural adhesion molecule L1 is phosphorylated on tyrosine and serine residues.

P C Heiland1, B Hertlein, O Traub, L S Griffith, B Schmitz.   

Abstract

The neural cell adhesion molecule L1 is highly homologous in its extracellular domain between species and completely identical in its cytoplasmic domain. We report here that tyrosine residues of L1 are phosphorylated in addition to serine residues, as determined by monoclonal phosphotyrosine antibodies and phosphoamino acid analysis. This result supports the suggestion that the cytoplasmic domain of L1 might be involved in signal transduction.

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Year:  1996        PMID： 8981445     DOI： 10.1097/00001756-199611040-00053

Source DB:  PubMed          Journal:  Neuroreport        ISSN： 0959-4965            Impact factor:   1.837


  4 in total

1.  Clinical mutations in the L1 neural cell adhesion molecule affect cell-surface expression.

Authors:  H D Moulding; R L Martuza; S D Rabkin
Journal:  J Neurosci       Date:  2000-08-01       Impact factor: 6.167

2.  A neuronal form of the cell adhesion molecule L1 contains a tyrosine-based signal required for sorting to the axonal growth cone.

Authors:  H Kamiguchi; V Lemmon
Journal:  J Neurosci       Date:  1998-05-15       Impact factor: 6.167

3.  The neural cell adhesion molecule L1 interacts with the AP-2 adaptor and is endocytosed via the clathrin-mediated pathway.

Authors:  H Kamiguchi; K E Long; M Pendergast; A W Schaefer; I Rapoport; T Kirchhausen; V Lemmon
Journal:  J Neurosci       Date:  1998-07-15       Impact factor: 6.167

4.  L1 endocytosis is controlled by a phosphorylation-dephosphorylation cycle stimulated by outside-in signaling by L1.

Authors:  Andrew W Schaefer; Yoshimasa Kamei; Hiroyuki Kamiguchi; Eric V Wong; Iris Rapoport; Tomas Kirchhausen; Carol M Beach; Gary Landreth; Sandra K Lemmon; Vance Lemmon
Journal:  J Cell Biol       Date:  2002-06-24       Impact factor: 10.539
  4 in total

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