Interaction of Caldesmon with Phospholipids

Overview

Journal Biochem J

Specialty Biochemistry

Date 1993 Apr 15

PMID 8484721

Citations 3

Authors

E A Czurylo

J ZBOROWSKI

R Dabrowska

Affiliations

Soon will be listed here.

Abstract

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (Kass. = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

Citing Articles

Intrinsically disordered caldesmon binds calmodulin via the "buttons on a string" mechanism.

Permyakov S, Permyakov E, Uversky V PeerJ. 2015; 3:e1265.

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Interaction of caldesmon with endoplasmic reticulum membrane: effects on the mobility of phospholipids in the membrane and on the phosphatidylserine base-exchange reaction.

Makowski P, Makuch R, Sikorski A, Jezierski A, Pikula S, Dabrowska R Biochem J. 1998; 328 ( Pt 2):505-9.

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Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments.

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