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Membrane-bound transcription factor site-2 protease

Introduction

Membrane-bound transcription factor site-2 protease, or site-2 protease (S2P) for short, is an enzyme (EC 3.4.24.85) encoded by the MBTPS2 gene which liberates the N-terminal fragment of sterol regulatory element-binding protein (SREBP) transcription factors from membranes.[1][2] S2P cleaves the transmembrane domain of SREPB, making it a member of the class of intramembrane proteases.

S2P endopeptidase (EC 3.4.24.85) is an enzyme.[3] This enzyme catalyses the following chemical reaction

Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP)-1, SREBP-2 and forms of the transcriptional activator ATF6.

This enzyme belongs to the peptidase family M50.

See also

See also

References

References

  1. ↑ Brown MS, Goldstein JL (1999). “A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood”. Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11041–8. doi:10.1073/pnas.96.20.11041. PMC 34238. PMID 10500120.
  2. ↑ Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, Hasan MT, Chang TY, Brown MS, Goldstein JL (1997). “Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs”. Mol. Cell. 1 (1): 47–57. doi:10.1016/S1097-2765(00)80006-4. PMID 9659902.
  3. ↑ Brown, M.S.; Ye, J.; Rawson, R.B.; Goldstein, J.L. (2000). “Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans”. Cell. 100: 391–398. doi:10.1016/S0092-8674(00)80675-3. PMID 10693756.
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