PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments

Yong Qian, Joseph M. Baisden, Lidia Cherezova, Justin M. Summy, Anne Guappone-Koay, Xianglin Shi, Tom Mast, Jennifer Pustula, Henry G. Zot, Nayef Mazloum, Marietta Y. Lee, Daniel C. Flynn

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

The actin filament-associated protein and Src-binding partner, AFAP-110, is an adaptor protein that links signaling molecules to actin filaments. AFAP-110 binds actin filaments directly and multimerizes through a leucine zipper motif. Cellular signals downstream of Src527F can regulate multimerization. Here, we determined recombinant AFAP-110 (rAFAP-110)-bound actin filaments cooperatively, through a lateral association. We demonstrate rAFAP-110 has the capability to cross-link actin filaments, and this ability is dependent on the integrity of the carboxy terminal actin binding domain. Deletion of the leucine zipper motif or PKC phosphorylation affected AFAP-110's conformation, which correlated with changes in multimerization and increased the capability of rAFAP-110 to cross-link actin filaments. AFAP-110 is both a substrate and binding partner of PKC. On PKC activation, stress filament organization is lost, motility structures form, and AFAP-110 colocalizes strongly with motility structures. Expression of a deletion mutant of AFAP-110 that is unable to bind PKC blocked the effect of PMA on actin filaments. We hypothesize that upon PKC activation, AFAP-110 can be cooperatively recruited to newly forming actin filaments, like those that exist in cell motility structures, and that PKC phosphorylation effects a conformational change that may enable AFAP-110 to promote actin filament cross-linking at the cell membrane.

Original languageEnglish
Pages (from-to)2311-2322
Number of pages12
JournalMolecular Biology of the Cell
Volume13
Issue number7
DOIs
Publication statusPublished - 2002
Externally publishedYes

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Actin Cytoskeleton
Phosphorylation
Leucine Zippers
AFAP 110
Protein Binding
Cell Movement
Actins
Cell Membrane

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Qian, Y., Baisden, J. M., Cherezova, L., Summy, J. M., Guappone-Koay, A., Shi, X., ... Flynn, D. C. (2002). PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. Molecular Biology of the Cell, 13(7), 2311-2322. https://doi.org/10.1091/mbc.E01-12-0148

PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. / Qian, Yong; Baisden, Joseph M.; Cherezova, Lidia; Summy, Justin M.; Guappone-Koay, Anne; Shi, Xianglin; Mast, Tom; Pustula, Jennifer; Zot, Henry G.; Mazloum, Nayef; Lee, Marietta Y.; Flynn, Daniel C.

In: Molecular Biology of the Cell, Vol. 13, No. 7, 2002, p. 2311-2322.

Research output: Contribution to journalArticle

Qian, Y, Baisden, JM, Cherezova, L, Summy, JM, Guappone-Koay, A, Shi, X, Mast, T, Pustula, J, Zot, HG, Mazloum, N, Lee, MY & Flynn, DC 2002, 'PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments', Molecular Biology of the Cell, vol. 13, no. 7, pp. 2311-2322. https://doi.org/10.1091/mbc.E01-12-0148
Qian, Yong ; Baisden, Joseph M. ; Cherezova, Lidia ; Summy, Justin M. ; Guappone-Koay, Anne ; Shi, Xianglin ; Mast, Tom ; Pustula, Jennifer ; Zot, Henry G. ; Mazloum, Nayef ; Lee, Marietta Y. ; Flynn, Daniel C. / PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. In: Molecular Biology of the Cell. 2002 ; Vol. 13, No. 7. pp. 2311-2322.
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