Abstract

Investigation into the structure and function of the nuclear lamina is proposed. Primary organisms of study will be Drosophila melanogaster and Saccharomyces cerevisiae. Sites of posttranslational modification of the Drosophila lamin will be mapped and the role of posttranslational modifications in regulating nuclear lamina form and function will be explored. In vitro mutagenesis of the cloned Drosophila lamin gene and in vivo genetic analyses will be employed in this effort. The biochemistry of nuclear lamina assembly and disassembly will be investigated using cell- free systems. The cloned Drosophila lamin gene will be expressed in the yeast, Saccharomyces cerevisiae. Posttranslational processing, subcellular localization and behavior during the cell cycle will be determined. The results of these investigations will add to our understanding of the maintenance of nuclear form and function during normal growth and in times of cellular stress (e.g. heat shock/hyperthermia), as well as during differentiation and development. Insights into the regulation of nuclear disassembly and reassembly in mitosis and meiosis are also anticipated.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM033132-08
Application #
3282457
Study Section
Molecular Cytology Study Section (CTY)
Project Start
1983-06-01
Project End
1995-03-31
Budget Start
1992-04-01
Budget End
1993-03-31
Support Year
8
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
State University New York Stony Brook
Department
Type
Schools of Medicine
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794

  Publications

Schneider, U; Mini, T; Jeno, P et al. (1999) Phosphorylation of the major Drosophila lamin in vivo: site identification during both M-phase (meiosis) and interphase by electrospray ionization tandem mass spectrometry. Biochemistry 38:4620-32
Goldberg, M; Lu, H; Stuurman, N et al. (1998) Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA. Mol Cell Biol 18:4315-23
Berrios, M; Fisher, P A; Matz, E C (1991) Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complexes. Proc Natl Acad Sci U S A 88:219-23
Lin, L; Fisher, P A (1990) Immunoaffinity purification and functional characterization of interphase and meiotic Drosophila nuclear lamin isoforms. J Biol Chem 265:12596-601
Smith, D E; Fisher, P A (1989) Interconversion of Drosophila nuclear lamin isoforms during oogenesis, early embryogenesis, and upon entry of cultured cells into mitosis. J Cell Biol 108:255-65
Fisher, P A; Smith, D E (1988) Affinity purification of antibodies using antigens immobilized on solid supports. Biochem Soc Trans 16:134-8
Gruenbaum, Y; Landesman, Y; Drees, B et al. (1988) Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene. J Cell Biol 106:585-96
Smith, D E; Gruenbaum, Y; Berrios, M et al. (1987) Biosynthesis and interconversion of Drosophila nuclear lamin isoforms during normal growth and in response to heat shock. J Cell Biol 105:771-90
Wu, L C; Fisher, P A; Broach, J R (1987) A yeast plasmid partitioning protein is a karyoskeletal component. J Biol Chem 262:883-91
McConnell, M; Whalen, A M; Smith, D E et al. (1987) Heat shock-induced changes in the structural stability of proteinaceous karyoskeletal elements in vitro and morphological effects in situ. J Cell Biol 105:1087-98

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