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Insulin‐induced stimulation of protein phosphorylation in Neurospora crassa cells
Author(s) -
Kole Hemanta K.,
Lenard John
Publication year - 1991
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.5.12.1717334
Subject(s) - neurospora crassa , phosphorylation , tyrosine , serine , biochemistry , protein phosphorylation , immunoprecipitation , biology , tyrosine phosphorylation , threonine , insulin receptor , microbiology and biotechnology , protein kinase a , insulin , mutant , insulin resistance , gene , endocrinology
1 ) Insulin stimulated the phosphorylation of at least 14 discrete proteins in Neurospora crassa cells. Specific proteins were phosphorylated at serine, threonine, and tyrosine residues, as determined by phosphoamino acid analysis of discrete spots on two‐dimensional gels. 2 ) Insulin stimulated the phosphorylation by [ γ ‐ 32 P]ATP of at least six discrete proteins in solubilized N. crassa membrane preparations at serine and tyrosine residues. 3 ) A phosphotyrosine‐containing protein of 38 kDa, pI 7.0–7.2, reacted by both immunoblotting and immunoprecipitation with antiserum to P2, a peptide from the human insulin receptor that contains an autophosphorylated tyrosine residue. In N. crassa cells, therefore, as in mammalian cells, insulin induces a variety of protein phosphorylations, some of which may be part of an evolutionarily conserved signal transduction pathway.—Kole, H. K.; Lenard, J. Insulin‐induced stimulation of protein phosphorylation in Neurospora crassa cells. FASEB J. 5: 2728‐2734; 1991.