Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling

Mark E Fortini

doi:10.1038/nrm910

Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling

Nat Rev Mol Cell Biol. 2002 Sep;3(9):673-84. doi: 10.1038/nrm910.

Author

Mark E Fortini¹

Affiliation

¹ Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Building 560, Room 22-12, Fort Detrick, Frederick, Maryland 21702, USA. fortini@ncifcrf.gov

PMID: 12209127
DOI: 10.1038/nrm910

Abstract

Many cell-surface receptors transmit signals to the nucleus through complex protein cascades. By contrast, the Notch signalling pathway uses a relatively direct mechanism, in which the intracellular domain of the receptor is liberated by intramembrane cleavage and translocates to the nucleus. This critical cleavage is mediated by the gamma-secretase complex, and new findings reveal that this mechanism is used by various receptors, although many questions remain about the biochemical details.

Publication types

Review

MeSH terms

Amyloid Precursor Protein Secretases
Animals
Aspartic Acid Endopeptidases
Cell Membrane / enzymology
Endopeptidases / chemistry
Endopeptidases / metabolism*
Humans
Macromolecular Substances
Membrane Proteins / metabolism*
Protein Processing, Post-Translational*
Protein Transport
Receptors, Cell Surface / metabolism*
Receptors, Notch
Signal Transduction*

Substances

Macromolecular Substances
Membrane Proteins
Receptors, Cell Surface
Receptors, Notch
Amyloid Precursor Protein Secretases
Endopeptidases
Aspartic Acid Endopeptidases
BACE1 protein, human