Literature DB >> 8484721

Interaction of caldesmon with phospholipids.

E A Czuryło1, J Zborowski, R Dabrowska.   

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.

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Year:  1993        PMID： 8484721      PMCID： PMC1132539          DOI： 10.1042/bj2910403

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  35 in total

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Journal:  Lipids       Date:  1970-05       Impact factor: 1.880

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Journal:  Biochem J       Date:  1992-06-15       Impact factor: 3.857

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Journal:  Proc Natl Acad Sci U S A       Date:  1981-09       Impact factor: 11.205

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  3 in total

1.  Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments.

Authors:  R Makuch; A Zasada; K Mabuchi; K Krauze; C L Wang; R Dabrowska
Journal:  Biophys J       Date:  1997-09       Impact factor: 4.033

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

Authors:  P Makowski; R Makuch; A F Sikorski; A Jezierski; S Pikula; R Dabrowska
Journal:  Biochem J       Date:  1997-12-01       Impact factor: 3.857

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

Authors:  Sergei E Permyakov; Eugene A Permyakov; Vladimir N Uversky
Journal:  PeerJ       Date:  2015-09-22       Impact factor: 2.984
  3 in total

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