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Calcium‐dependent interaction of annexin I with annexin II and mapping of the interaction sites
Author(s) -
Lee Kyoung Hoa,
Na Doe Sun,
Kim Jung Woo
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01643-3
Subject(s) - annexin , annexin a2 , c2 domain , hela , two hybrid screening , complementary dna , protein–protein interaction , domain (mathematical analysis) , chemistry , calcium binding protein , cdna library , microbiology and biotechnology , intracellular , in vitro , biology , biochemistry , calcium , yeast , gene , mathematical analysis , mathematics , organic chemistry , membrane
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.