Localization of phospholipid-binding sites of caldesmon

Natalia Bogatcheva, Pia A J Huber, Iain D C Fraser, Steven B. Marston, Nikolai B. Gusev

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The interaction of phosphatidylserine with intact smooth muscle caldesmon and caldesmon fragments obtained by bacterial expression was investigated by means of light scattering. Among these fragments only those derived from the C-terminal part of caldesmon (so-called domain 4) were able to interact with phospholipids. Fragments 606C (residues 606-756), H7 (566-710) and H2 (626-710) form tight complexes with phosphatidylserine, whereas fragments H8 (658-737), H9 (669-737) and fragment H4 (566-624) interact with phospholipids less effectively. It is concluded that the phospholipid-binding site is located in the sequence 626-710 of caldesmon. This sequence contains calmodulin-binding sites and serine residues phosphorylated by protein kinase C and pro-directed protein kinases. This could explain the effects of calmodulin and phosphorylation on the caldesmon-phospholipid interaction described earlier.

Original languageEnglish (US)
Pages (from-to)176-180
Number of pages5
JournalFEBS Letters
Volume342
Issue number2
DOIs
StatePublished - Apr 4 1994
Externally publishedYes

Fingerprint

Calmodulin-Binding Proteins
Phospholipids
Binding Sites
Phosphatidylserines
Calmodulin
Phosphorylation
Light scattering
Protein Kinases
Serine
Protein Kinase C
Smooth Muscle
Muscle
Light

Keywords

  • Caldesmon
  • Calmodulin
  • phospholipid
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Bogatcheva, N., Huber, P. A. J., Fraser, I. D. C., Marston, S. B., & Gusev, N. B. (1994). Localization of phospholipid-binding sites of caldesmon. FEBS Letters, 342(2), 176-180. https://doi.org/10.1016/0014-5793(94)80495-8

Localization of phospholipid-binding sites of caldesmon. / Bogatcheva, Natalia; Huber, Pia A J; Fraser, Iain D C; Marston, Steven B.; Gusev, Nikolai B.

In: FEBS Letters, Vol. 342, No. 2, 04.04.1994, p. 176-180.

Research output: Contribution to journalArticle

Bogatcheva, N, Huber, PAJ, Fraser, IDC, Marston, SB & Gusev, NB 1994, 'Localization of phospholipid-binding sites of caldesmon', FEBS Letters, vol. 342, no. 2, pp. 176-180. https://doi.org/10.1016/0014-5793(94)80495-8
Bogatcheva, Natalia ; Huber, Pia A J ; Fraser, Iain D C ; Marston, Steven B. ; Gusev, Nikolai B. / Localization of phospholipid-binding sites of caldesmon. In: FEBS Letters. 1994 ; Vol. 342, No. 2. pp. 176-180.
@article{f62d01df88014df281aab88e1781b952,
title = "Localization of phospholipid-binding sites of caldesmon",
abstract = "The interaction of phosphatidylserine with intact smooth muscle caldesmon and caldesmon fragments obtained by bacterial expression was investigated by means of light scattering. Among these fragments only those derived from the C-terminal part of caldesmon (so-called domain 4) were able to interact with phospholipids. Fragments 606C (residues 606-756), H7 (566-710) and H2 (626-710) form tight complexes with phosphatidylserine, whereas fragments H8 (658-737), H9 (669-737) and fragment H4 (566-624) interact with phospholipids less effectively. It is concluded that the phospholipid-binding site is located in the sequence 626-710 of caldesmon. This sequence contains calmodulin-binding sites and serine residues phosphorylated by protein kinase C and pro-directed protein kinases. This could explain the effects of calmodulin and phosphorylation on the caldesmon-phospholipid interaction described earlier.",
keywords = "Caldesmon, Calmodulin, phospholipid, Phosphorylation",
author = "Natalia Bogatcheva and Huber, {Pia A J} and Fraser, {Iain D C} and Marston, {Steven B.} and Gusev, {Nikolai B.}",
year = "1994",
month = "4",
day = "4",
doi = "10.1016/0014-5793(94)80495-8",
language = "English (US)",
volume = "342",
pages = "176--180",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Localization of phospholipid-binding sites of caldesmon

AU - Bogatcheva, Natalia

AU - Huber, Pia A J

AU - Fraser, Iain D C

AU - Marston, Steven B.

AU - Gusev, Nikolai B.

PY - 1994/4/4

Y1 - 1994/4/4

N2 - The interaction of phosphatidylserine with intact smooth muscle caldesmon and caldesmon fragments obtained by bacterial expression was investigated by means of light scattering. Among these fragments only those derived from the C-terminal part of caldesmon (so-called domain 4) were able to interact with phospholipids. Fragments 606C (residues 606-756), H7 (566-710) and H2 (626-710) form tight complexes with phosphatidylserine, whereas fragments H8 (658-737), H9 (669-737) and fragment H4 (566-624) interact with phospholipids less effectively. It is concluded that the phospholipid-binding site is located in the sequence 626-710 of caldesmon. This sequence contains calmodulin-binding sites and serine residues phosphorylated by protein kinase C and pro-directed protein kinases. This could explain the effects of calmodulin and phosphorylation on the caldesmon-phospholipid interaction described earlier.

AB - The interaction of phosphatidylserine with intact smooth muscle caldesmon and caldesmon fragments obtained by bacterial expression was investigated by means of light scattering. Among these fragments only those derived from the C-terminal part of caldesmon (so-called domain 4) were able to interact with phospholipids. Fragments 606C (residues 606-756), H7 (566-710) and H2 (626-710) form tight complexes with phosphatidylserine, whereas fragments H8 (658-737), H9 (669-737) and fragment H4 (566-624) interact with phospholipids less effectively. It is concluded that the phospholipid-binding site is located in the sequence 626-710 of caldesmon. This sequence contains calmodulin-binding sites and serine residues phosphorylated by protein kinase C and pro-directed protein kinases. This could explain the effects of calmodulin and phosphorylation on the caldesmon-phospholipid interaction described earlier.

KW - Caldesmon

KW - Calmodulin

KW - phospholipid

KW - Phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0028330857&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028330857&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(94)80495-8

DO - 10.1016/0014-5793(94)80495-8

M3 - Article

VL - 342

SP - 176

EP - 180

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -