The mechanism of cell surface recognition, adhesion, and deadhesion will be studied in the biflagellated alga Chlamydomonas reinhardtii. During the mating reaction, gametes of opposite mating types adhere to each other via their flagella and ultimately fuse to form zygotes. This adhesive interaction is accompanied by a simultaneous de-adhesion event which, in the presence of protein synthesis inhibitors or an inhibitor of protein glycosylation, leads to loss of adhesiveness of the interacting flagella and disaggregation of the gametes. The long-term goal is to understand the molecular mechanisms of adhesion and deadhesion. The research described in the present application is intended to accomplish the following: 1) the identification, purification, and biochemical characterization of the antigen to which a recently prepared adhesion blocking monoclonal antibody is directed; 2) the characterization of the cellular location and behavior of the antigen before, during, and after mating; 3) the identification and purification, using standard biochemical methods, of flagellar adhesion molecules and comparison of these molecules to the antigen described in 1 and 2; 4) initiation of studies on the molecular biology of adhesion with the immediate objective of learning the methods and vocabulary of this approach and the longer-term objective of cloning genes for adhesion molecules.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM025661-12
Application #
3273198
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1978-07-01
Project End
1990-07-31
Budget Start
1989-08-01
Budget End
1990-07-31
Support Year
12
Fiscal Year
1989
Total Cost
Indirect Cost
Name
University of Texas Sw Medical Center Dallas
Department
Type
Overall Medical
DUNS #
City
Dallas
State
TX
Country
United States
Zip Code
75390
Cao, Muqing; Ning, Jue; Hernandez-Lara, Carmen I et al. (2015) Uni-directional ciliary membrane protein trafficking by a cytoplasmic retrograde IFT motor and ciliary ectosome shedding. Elife 4:
Haubrich, Brad A; Collins, Emily K; Howard, Alicia L et al. (2015) Characterization, mutagenesis and mechanistic analysis of an ancient algal sterol C24-methyltransferase: Implications for understanding sterol evolution in the green lineage. Phytochemistry 113:64-72
Pan, Junmin; Snell, William J (2014) Organelle size: a cilium length signal regulates IFT cargo loading. Curr Biol 24:R75-8
Cao, Muqing; Meng, Dan; Wang, Liang et al. (2013) Activation loop phosphorylation of a protein kinase is a molecular marker of organelle size that dynamically reports flagellar length. Proc Natl Acad Sci U S A 110:12337-42
Belzile, Olivier; Hernandez-Lara, Carmen I; Wang, Qian et al. (2013) Regulated membrane protein entry into flagella is facilitated by cytoplasmic microtubules and does not require IFT. Curr Biol 23:1460-5
Ning, Jue; Otto, Thomas D; Pfander, Claudia et al. (2013) Comparative genomics in Chlamydomonas and Plasmodium identifies an ancient nuclear envelope protein family essential for sexual reproduction in protists, fungi, plants, and vertebrates. Genes Dev 27:1198-215
Miller, Matthew B; Haubrich, Brad A; Wang, Qian et al. (2012) Evolutionarily conserved Delta(25(27))-olefin ergosterol biosynthesis pathway in the alga Chlamydomonas reinhardtii. J Lipid Res 53:1636-45
Luo, Minna; Cao, Muqing; Kan, Yinan et al. (2011) The phosphorylation state of an aurora-like kinase marks the length of growing flagella in Chlamydomonas. Curr Biol 21:586-91
Rohatgi, Rajat; Snell, William J (2010) The ciliary membrane. Curr Opin Cell Biol 22:541-6
Piao, Tian; Luo, Minna; Wang, Liang et al. (2009) A microtubule depolymerizing kinesin functions during both flagellar disassembly and flagellar assembly in Chlamydomonas. Proc Natl Acad Sci U S A 106:4713-8

Showing the most recent 10 out of 41 publications