Abstract
Protein-tyrosine phosphatase 1B (PTP1B) has emerged as an important regulator of several signaling networks that are implicated in human metabolic diseases such as diabetes and obesity. A growing body of evidence demonstrates that PTP1B displays exquisite substrate specificity. In this chapter we review mechanisms that regulate PTP1B-susbtrate interactions and highlight substrates that mediate PTP1B metabolic actions. PTP1B-substrate interactions are modulated by PTP1B subcellular location and numerous posttranslational modifications that regulate its activity such as oxidation, nitrosylation, sulfhydration, sumoylation, phosphorylation, and proteolysis. The metabolic actions of PTP1B are mediated by key physiological substrates that regulate insulin and leptin signaling, cell-cell communication, and endoplasmic reticulum (ER) stress response.
| Original language | English (US) |
|---|---|
| Title of host publication | Protein Tyrosine Phosphatase Control of Metabolism |
| Publisher | Springer New York |
| Pages | 49-69 |
| Number of pages | 21 |
| ISBN (Print) | 9781461478553, 1461478545, 9781461478546 |
| DOIs | |
| State | Published - Apr 1 2013 |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Protein-tyrosine phosphatase 1B substrates and control of Metabolism. / Xi, Yannan; Haj, Fawaz.
Protein Tyrosine Phosphatase Control of Metabolism. Springer New York, 2013. p. 49-69.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Protein-tyrosine phosphatase 1B substrates and control of Metabolism
AU - Xi, Yannan
AU - Haj, Fawaz
PY - 2013/4/1
Y1 - 2013/4/1
N2 - Protein-tyrosine phosphatase 1B (PTP1B) has emerged as an important regulator of several signaling networks that are implicated in human metabolic diseases such as diabetes and obesity. A growing body of evidence demonstrates that PTP1B displays exquisite substrate specificity. In this chapter we review mechanisms that regulate PTP1B-susbtrate interactions and highlight substrates that mediate PTP1B metabolic actions. PTP1B-substrate interactions are modulated by PTP1B subcellular location and numerous posttranslational modifications that regulate its activity such as oxidation, nitrosylation, sulfhydration, sumoylation, phosphorylation, and proteolysis. The metabolic actions of PTP1B are mediated by key physiological substrates that regulate insulin and leptin signaling, cell-cell communication, and endoplasmic reticulum (ER) stress response.
AB - Protein-tyrosine phosphatase 1B (PTP1B) has emerged as an important regulator of several signaling networks that are implicated in human metabolic diseases such as diabetes and obesity. A growing body of evidence demonstrates that PTP1B displays exquisite substrate specificity. In this chapter we review mechanisms that regulate PTP1B-susbtrate interactions and highlight substrates that mediate PTP1B metabolic actions. PTP1B-substrate interactions are modulated by PTP1B subcellular location and numerous posttranslational modifications that regulate its activity such as oxidation, nitrosylation, sulfhydration, sumoylation, phosphorylation, and proteolysis. The metabolic actions of PTP1B are mediated by key physiological substrates that regulate insulin and leptin signaling, cell-cell communication, and endoplasmic reticulum (ER) stress response.
UR - http://www.scopus.com/inward/record.url?scp=84929545427&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84929545427&partnerID=8YFLogxK
U2 - 10.1007/978-1-4614-7855-3_3
DO - 10.1007/978-1-4614-7855-3_3
M3 - Chapter
AN - SCOPUS:84929545427
SN - 9781461478553
SN - 1461478545
SN - 9781461478546
SP - 49
EP - 69
BT - Protein Tyrosine Phosphatase Control of Metabolism
PB - Springer New York
ER -