Calcium-dependent interaction of annexin I with annexin II and mapping of the interaction sites.

Abstract:

:Annexins are multifunctional intracellular proteins with Ca2+- 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 Ca2+-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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lee KH,Na DS,Kim JW

doi

10.1016/s0014-5793(98)01643-3

subject

Has Abstract

pub_date

1999-01-15 00:00:00

pages

143-6

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01643-3

journal_volume

442

pub_type

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