Calcium, protease action, and the regulation of the cell cycle

Luigia Santella, Keiichiro Kyozuka, Laura De Riso, Ernesto Carafoli

Research output: Contribution to journalReview articlepeer-review

67 Citations (Scopus)

Abstract

Proteolysis is a key event in the control of the cell cycle. Most of the proteins which are degraded at specific cycle points, e.g. cyclins A, B, and E, are substrates of the ubiquitin/proteasome pathway. The Ca2+ dependent neutral protease calpain also cleaves cell cycle proteins, among them cyclin D1 and the c-mos proto-oncogene product which is a component of the CSF. The proteasome itself, however, may be under Ca2+ control through the binding of Ca2+ to its 29 kDa regulatory subunit. Calpain undergoes relocation among cell compartments during the various steps of the mitotic and meiotic cycles. It promotes the initiation and the progression of mitosis when injected into the perinuclear space of synchronized PtK, cells, and the resumption of meiosis when directly injected into the nuclei of prophase-arrested starfish oocytes. Apart from the proteins mentioned above, most of the substrates of calpain which become cleaved during mitosis and meiosis are still unknown. Microtubule-associated proteins are likely candidates.

Original languageEnglish
Pages (from-to)123-130
Number of pages8
JournalCell Calcium
Volume23
Issue number2-3
DOIs
Publication statusPublished - 1998 Jan 1

ASJC Scopus subject areas

  • Physiology
  • Molecular Biology
  • Cell Biology

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