Annexins as intracellular calcium sensors

Monastyrskaya, Katia; Babiychuk, Eduard B; Hostettler, Andrea; Rescher, Ursula; Draeger, Annette (2007). Annexins as intracellular calcium sensors. Cell calcium, 41(3), pp. 207-19. Amsterdam: Elsevier 10.1016/j.ceca.2006.06.008

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The annexins are a multigene family of Ca(2+)- and charged phospholipid-binding proteins. Although they have been ascribed with diverse functions, there is no consensus about the role played by this family as a whole. We have mapped the Ca(2+)-induced translocations of four members of the annexin family and of two truncated annexins in live cells, and demonstrated that these proteins interact with the plasma membrane as well as with internal membrane systems in a highly coordinated manner. Annexin 2 was the most Ca(2+) sensitive of the studied proteins, followed by annexins 6, 4 and 1. The calcium sensitivity of annexin 2 increased further following co-expression with S100A10. Upon elevation of [Ca(2+)](i), annexins 2 and 6 translocated to the plasma membrane, whereas annexins 4 and 1 also became associated with intracellular membranes and the nuclear envelope. The NH(2)-terminus had a modulatory effect on plasma membrane binding: its truncation increased the Ca(2+) sensitivity of annexin 1, and decreased that of annexin 2. Given the fact that several annexins are present within any one cell, it is likely that they form a sophisticated [Ca(2+)] sensing system, with a regulatory influence on other signaling pathways.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy > Cell Biology
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy

UniBE Contributor:

Monastyrskaya-Stäuber, Katia; Babiychuk, Eduard; Hostettler, Andrea and Draeger, Annette

ISSN:

0143-4160

ISBN:

16914198

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:46

Last Modified:

04 May 2014 23:13

Publisher DOI:

10.1016/j.ceca.2006.06.008

PubMed ID:

16914198

Web of Science ID:

000244770700002

URI:

https://boris.unibe.ch/id/eprint/18921 (FactScience: 1192)

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