Targeted fusion proteins and methods for the...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Reexamination Certificate

active

06838263

ABSTRACT:
Cell membranes containing glycolipid-enriched membrane (GEM) and non-glycolipid-enriched membrane (non-GEM) domains are targeted using fusion proteins that are anchored in the cell membrane. Fusion proteins to target GEM (or non-GEM) domains are comprised of a selected fluorescent polypeptide, a membrane-targeting sequence of p56Lck(or pp60c-Srcfor non-GEM domains) and a linker inserted between the polypeptide and the membrane targeting sequence. Localization of fusion proteins in GEM and non-GEM domains is assessed using techniques including confocal microscopy, fluorescence-based techniques, and membrane fractionation. Using these techniques, compounds are screened for their effect on GEM and non-GEM domains of live cells. These fusion proteins therefore represent useful tools for studying subcellular trafficking and the function of discrete compartments in the plasma membrane.

REFERENCES:
patent: 6342379 (2002-01-01), Tsien et al.
patent: 20020076729 (2002-06-01), Meyer et al.
patent: 20030066095 (2003-04-01), Baubet et al.
Anders et al., “Effects of c-Src tyrosine kinase on ethanol sensitivity of recombinant NMDA receptors expressed in HEK 293 cells,”Alocoholism, Clinical and Experimental Research, 23(2):357-362, 1999.
Bijlmakers and Marsh, “Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck),”Molecular Biology of the Cell, 11(5):1585-1595, 2000.
Brown and London, “Functions of lipid rafts in biological membranes,”Annu. Rev. Cell Dev. Biol., 14:111-136, 1998.
Buckland et al., “Co-ordination of the expression of the protein tyrosine kinase p56(lck) with the pre-T cell receptor during thymocyte development,”European Journal of Immunology, 30(1):8-18, 2000.
Chiu et al., “Trafficking of spontaneously endocytosed MHC proteins,”Proc. Natl. Acad. Sci. USA, 96(24):13944-13949, 1999.
Janes et al., “Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor,”J. of Cell Biology, 147(2):447-461, 1999.
Kabouridis et al., “S-acylation of LCK protein tyrosine kinase is essential for its signaling function in T lymphocytes,”Embo. J., 16(16):4983-4998, 1997.
Karnitz et al., “Effects of p56lckdeficiency on the growth and cytolytic effector functionof an interleukin-2-dependent cytotoxic T-cell line,”Mol. Cell Biol.,12:4521-4530, 1992.
Kwong and Lublin, “Amino-terminal palmitate of polybasic domain can provide required second signal to myristate for membrane binding of p56lck,”Biochem. Biophys. Res. Commun., 207(2):868-876, 1995.
McCabe and Berthiaume, “Functional roles for fatty acylated amino-terminal domains in subcellular localization,”Molecular Biology of the Cell, 10:3771-3786, 1999.
Nichols et al., “Rapid cycling of lipid raft markers between the cell surface and Golgi complex,”J. of Cell Biology, 153(3):529-541, 2001.
Pyenta et al., “Cross-correlation analysis of inner-leaflet-anchored green fluorescent protein co-redistributed with Ige receptors and outer leaflet lipid raft components,”Biophysical Journal, 80(5):2120-2132, 2001.
Resh, “Myristylation and palmitylation of Src family members: the fats of the matter,”Cell, 76:411-413, 1994.
Rodgers and Rose, “Exclusion of CD45 inhibits activity of p56lckassociated with glycolipid-enriched membrane domains,”J. Cell Biol., 135:1515-1523, 1996.
Rodgers et al., “Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction,”Mol. Cell Biol., 14:5384-5391, 1994.
Shenoy-Scaria et al., “Cysteine3of Src family tyrosine kinases determines palmitoylation and localization in caveolae,”J. Cell Biol., 126:353-363, 1994.
Shenoy-Scaria et al., “Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lckand p59fynmediates interaction with glycosyl-phosphatidylinositol-anchored proteins,”Mol. Cell Biol., 13:6385-6392, 1993.
Simons and Toomre, “Lipid rafts and signal transduction,”Nature Rev. Mol. Cell Biol., 1:31-39, 2000.
Straus and Weiss, “Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor,”Cell, 70:585-593, 1992.
Tansey et al., “GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival,”Neuron, 25(3):611-623, 2000.
Xavier et al., “Membrane compartmentation is required for efficient T cell activation,”Immunity, 8:723-732, 1998.
Yurchak and Sefton, “Palmitoylation of either Cys-3 or Cys-5 is required for the biological activity of the Lck tyrosine protein kinase,”Mol. Cell Biol.,15:6914-6922, 1995.
Zacharias et al., “Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells,”Science, 296:913-916, 2002.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Targeted fusion proteins and methods for the... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Targeted fusion proteins and methods for the..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Targeted fusion proteins and methods for the... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3388479

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.