Abstract
In recent years it has become apparent that an increasing number of proteins can be phosphorylated at several different sites. In this article protein multisite phosphorylation is discussed with reference to the enzymes glycogen synthase, pyruvate dehydrogenase, and phosphorylase kinase. Each of these enzymes contains three or more different phosphorylation sites on one or more subunits. Activation and inactivation of the enzymes appear to correlate quite well with phosphorylation of a few key sites on the protein. The other phosphorylation sites may influence other kinetic properties of the enzymes or regulate the rates of dephosphorylation of the key sites by the appropriate phosphatase. Thus, multisite phosphorylation may represent an important mechanism for regulating several functions of complex proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 157-179 |
| Number of pages | 23 |
| Journal | Molecular and Cellular Endocrinology |
| Volume | 16 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1979 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Endocrinology
- Endocrinology, Diabetes and Metabolism
Cite this
Regulatory functions of protein multisite phosphorylation. / Soderling, Thomas.
In: Molecular and Cellular Endocrinology, Vol. 16, No. 3, 1979, p. 157-179.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulatory functions of protein multisite phosphorylation
AU - Soderling, Thomas
PY - 1979
Y1 - 1979
N2 - In recent years it has become apparent that an increasing number of proteins can be phosphorylated at several different sites. In this article protein multisite phosphorylation is discussed with reference to the enzymes glycogen synthase, pyruvate dehydrogenase, and phosphorylase kinase. Each of these enzymes contains three or more different phosphorylation sites on one or more subunits. Activation and inactivation of the enzymes appear to correlate quite well with phosphorylation of a few key sites on the protein. The other phosphorylation sites may influence other kinetic properties of the enzymes or regulate the rates of dephosphorylation of the key sites by the appropriate phosphatase. Thus, multisite phosphorylation may represent an important mechanism for regulating several functions of complex proteins.
AB - In recent years it has become apparent that an increasing number of proteins can be phosphorylated at several different sites. In this article protein multisite phosphorylation is discussed with reference to the enzymes glycogen synthase, pyruvate dehydrogenase, and phosphorylase kinase. Each of these enzymes contains three or more different phosphorylation sites on one or more subunits. Activation and inactivation of the enzymes appear to correlate quite well with phosphorylation of a few key sites on the protein. The other phosphorylation sites may influence other kinetic properties of the enzymes or regulate the rates of dephosphorylation of the key sites by the appropriate phosphatase. Thus, multisite phosphorylation may represent an important mechanism for regulating several functions of complex proteins.
UR - http://www.scopus.com/inward/record.url?scp=0018583208&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018583208&partnerID=8YFLogxK
U2 - 10.1016/0303-7207(79)90024-8
DO - 10.1016/0303-7207(79)90024-8
M3 - Article
VL - 16
SP - 157
EP - 179
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
SN - 0303-7207
IS - 3
ER -