Literature DB >> 8439308

Chicken and mouse focal adhesion kinases are similar in structure at their amino termini.

B B Devor1, X Zhang, S K Patel, T R Polte, S K Hanks.   

Abstract

A novel protein-tyrosine kinase, designated 'Focal Adhesion Kinase' (FAK), has recently been implicated in signal transduction pathways activated by extracellular adhesion molecules and by neuropeptide growth factors. Previously deduced primary structures for chicken and mouse FAK polypeptides differ at their amino-termini, with mouse FAK reported to have a 25 amino acid residue extension not present in chicken FAK. Additional sequence information from the 5'-end region of the chicken FAK transcript now indicates that the amino-terminal extension previously thought to be unique to mouse FAK is, in fact, also predicted for chicken FAK. Thus mouse and chicken FAK polypeptides appear to be structurally similar throughout their lengths. This is further supported by comparison of their electrophoretic mobilities.

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Year:  1993        PMID: 8439308     DOI: 10.1006/bbrc.1993.1160

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Mapping of the focal adhesion kinase (Fadk) gene to mouse chromosome 15 and human chromosome 8.

Authors:  F T Fiedorek; E S Kay
Journal:  Mamm Genome       Date:  1995-02       Impact factor: 2.957

2.  Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases.

Authors:  M B Calalb; T R Polte; S K Hanks
Journal:  Mol Cell Biol       Date:  1995-02       Impact factor: 4.272

  2 in total

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