Abstract

The long range goal of these investigators is to determine the influence of the actin-bound divalent cation and bound nucleotide: (1) on the characteristics of both monomer and polymer actin; (2) on the polymerization mechanism of actin; and (3) on the interaction of actin with actin-associated proteins. The research will specifically address the effects of actin-associated proteins on the characteristics and polymerization properties of actin that they have been studying.
The specific aims are as follows: (1) the capping of actin polymers by gelsolin and gCap39 will be studied; (2) the mechanism of actin filament severing by gelsolin will be investigated under physiological conditions; (3) the effect of gelsolin on the nucleation of actin polymerization will be clarified; (4) the effect of profilin on actin-bound nucleotide exchange and on actin polymerization will be studied; (5) the influence of thymosin beta4 on bound nucleotide exchange, on actin, and on actin polymerization will be determined; (6) actin filament dynamics and actin-bound nucleotide exchange in ensembles of actin and combinations of all three actin-associated proteins, gelsolin, profilin and thymosin beta4 will be investigated.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM032007-11
Application #
2021953
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1985-05-01
Project End
1998-12-31
Budget Start
1997-01-01
Budget End
1998-12-31
Support Year
11
Fiscal Year
1997
Total Cost
Indirect Cost

  Institution

Name
Albany Medical College
Department
Physiology
Type
Schools of Medicine
DUNS #
City
Albany
State
NY
Country
United States
Zip Code
12208

  Publications

Selden, L A; Kinosian, H J; Estes, J E et al. (1999) Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics. Biochemistry 38:2769-78
Kinosian, H J; Newman, J; Lincoln, B et al. (1998) Ca2+ regulation of gelsolin activity: binding and severing of F-actin. Biophys J 75:3101-9
Selden, L A; Kinosian, H J; Newman, J et al. (1998) Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin. Biophys J 75:3092-100
Kinosian, H J; Selden, L A; Estes, J E et al. (1996) Kinetics of gelsolin interaction with phalloidin-stabilized F-actin. Rate constants for binding and severing. Biochemistry 35:16550-6
Gershman, L C; Selden, L A; Kinosian, H J et al. (1994) Actin-bound nucleotide/divalent cation interactions. Adv Exp Med Biol 358:35-49
Selden, L A; Kinosian, H J; Estes, J E et al. (1994) Influence of the high affinity divalent cation on actin tryptophan fluorescence. Adv Exp Med Biol 358:51-7
Kinosian, H J; Selden, L A; Estes, J E et al. (1993) Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates. J Biol Chem 268:8683-91
Newman, J; Zaner, K S; Schick, K L et al. (1993) Nucleotide exchange and rheometric studies with F-actin prepared from ATP- or ADP-monomeric actin. Biophys J 64:1559-66
Herrmannsdoerfer, A J; Heeb, G T; Feustel, P J et al. (1993) Vascular clearance and organ uptake of G- and F-actin in the rat. Am J Physiol 265:G1071-81
Kinosian, H J; Selden, L A; Estes, J E et al. (1993) Actin filament annealing in the presence of ATP and phalloidin. Biochemistry 32:12353-7

Showing the most recent 10 out of 20 publications