Premium
Substrates and signalling complexes: The tortured path to insulin action
Author(s) -
Roth Richard A.,
Zhang Bei,
Chin Janice E.,
Kovacina Kristina
Publication year - 1992
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240480104
Subject(s) - autophosphorylation , insulin receptor , biochemistry , receptor tyrosine kinase , tyrosine phosphorylation , phosphorylation , microbiology and biotechnology , irs2 , biology , tyrosine kinase , chemistry , signal transduction , protein kinase a , insulin , insulin resistance , endocrinology
In the last few years several potential substrates of the insulin receptor tyrosine kinase have been identified, purified, and their cDNAs isolated. These putative substrates include: (1) pp15, a fatty acid‐binding protein; (2) pp120, a plasma membrane ecto‐ATPase; (3) pp42, a MAP serine/threonine kinase; (4) pp85, a subunit of the Type 1 phosphatidylinositol kinase; and (5) pp185, a phosphatidylinositol kinase binding protein. Although the tyrosine phosphorylation of several of these substrates correlates with the signalling capabilities of various mutant receptors, the role of these substrates in mediating any one of insulin's many biological responses is still unknown. In addition, recent data indicate that the tyrosine phosphorylation of pp42 may in fact be due to autophosphorylation, thereby removing it from the list of putative substrates of the insulin receptor kinase. Finally, the present review discusses the question of whether signalling occurs as a result of the tyrosine phosphorylation of substrates or via the formation of signalling complexes.