In:
FEBS Letters, Wiley, Vol. 442, No. 2-3 ( 1999-01-15), p. 143-146
Abstract:
Annexins are multifunctional intracellular proteins with Ca 2+ ‐ and phospholipid‐binding properties. Their structures consist of four conserved repeat domains that form the core and a diverse N‐terminal tail, from which their functional differences may arise. We searched for cellular proteins that interact with the N‐terminal tail plus domain I of annexin I (ANX1) by using the yeast two‐hybrid method. Screening of a HeLa cell cDNA library yielded annexin II (ANX2) cDNA. The interaction between ANX1 and ANX2 also occurred in vitro in a Ca 2+ ‐dependent manner. Mapping of the interaction sites revealed that interaction between domain I of ANX1 and domain IV of ANX2 was stronger than the other combinations.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(98)01643-3
Language:
English
Publisher:
Wiley
Publication Date:
1999
detail.hit.zdb_id:
1460391-3
SSG:
12
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