Protein-protein interactions of p66 ShcA

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S350000

Reexamination Certificate

active

07056684

ABSTRACT:
The present invention relates to (a) the establishment of a direct consequence to the mitochondrial import of phosphorylated p66ShcAand its association with prohibitin, and (b) to a potential function for the prohibitin-p66ShcAcomplex in the mitochondrial membrane depolarization process that governs metabolic events such as bioenergetics and free radical formation. The present invention can also be employed as a tool for identifying pharmaceutically active compounds that disrupt the prohibitin-p66ShcAinteraction, thereby providing treatment options for aging-related diseases such as diabetes, cardiovascular, osteoporosis, cancer and neurodegenerative diseases.

REFERENCES:
Sutovsky, P. et al, “Ubiquitinated Sperm Mitochondria, Selective Proteolysis, and the Regulation of Mitochondrial Inheritance in Mammalian Embryos”, Biology of Reproduction, vol. 63, pp. 582-590 (2000).
Coates, P.J. et al, “Mammalian Prohibitin Proteins Respond to Mitochondrial Stress and Decrease during Cellular Senescence”, Experimental Cell Research, vol. 265, pp. 262-273 (2001).
Sehnke, P.C. et al, “Interaction of a Plant 14-3-3 Protein with the Signal Peptide of a Thylakoid-Targeted Chloroplast Precursor Protein and the Presence of 14-3-3 Isoforms in the Chloroplast Stroma”, Plant Physiology, vol. 122, pp. 235-241 (2000).
Jackson, J. et al, “Elevated Levels of p66 Shc Are Found in Breast Cancer Cell Lines and Primary Tumors with High Metastatic Potential”, Clin. Cancer Res., vol. 6, pp. 1135-1139 (2000).
El-Shemerly, M. et al. “12-O-Tetradecanoylphorbol-13-acetate Activates the Ras/Extracellular Signal-regulated Kinase (ERK) Signaling Pathway Upstream of SOS Involving Serince Phosphorylation of Shc in NIH3T3 Cells”, J. of Biological Chem., pp. 30599-30602 (1997).
Bonfini, L. et al, “Not all Shc's roads lead to Ras”, TIBS, vol. 21, pp. 257-261 (1996).
Migliaccio, E. et al, “The p66shc adaptor protein controls oxidative stress response and life span in mammals”, Nature, vol. 402, pp. 309-313 (1999).
Migliaccio, E. et al, “Opposite effects of the p52shc/p46shcand p66shcsplicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway”, EMBO J., vol. 16, No. 4, pp. 706-716 (1997).
Downward, Julian, “The GRB2/SEM-5 adaptor protein”, FEBS Letters, vol. 338, pp. 113-117 (1994).
Kao, A. et al, “Insulin Stimulates the Phosphorylation of the 66- and 52-Kilodalton Shc Isoforms by Distinct Pathways”, Endocrinology, vol. 138, No. 6, pp. 2474-2480 (1997).
Foschi, M. et al, “Endothelin-1 Induces Serine Phosphorylation of the Adaptor Protein p66Shcand Its Association with 14-3-3 Protein in Glomerular Mesangial Cells”, J. of Biol. Chemistry, vol. 276, No. 28, pp. 26640-26647 (2001).
Yang, C. et al, “Taxol Mediates Serin e Phosphorylation of the 66-kDa Shc Isoform” Cancer Res., vol. 60, pp. 5171-5178 (2000).
Tavernarakis, N. et al, The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins, TIBS, pp. 425-427 (1999).
Langer, T. et al, “AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis”, Biochem. Soc. Trans., vol. 29, part 4, pp. 431-436 (2001).
Wang, S. et al, “Rb and Prohibitin Target Distinct Regions of E2F1 for Repression and Respond to Different Upstream Signals”, Molecular Cell. Biol., vol. 19, No. 11, pp. 7447-7460 (1999).
Coates, P. et al, Mammalian Prohibitin Proteins Respond to Mitochondrial Stress and Decrease during Cellular Senescence, Experimental Cell Res., vol. 265, pp. 262-273 (2001).
Nijtmans, L. et al, “The mitochondrial PHB complex:roles in mitochondrial respiratory complex assemby, ageing and degenerative disease”, CMLS, Cell Mol. Life Sci., vol. 59, pp. 143-155 (2002).
Nijtmans, L. et al, “Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins”, EMBO J., vol. 19, No. 11, pp. 2444-2451 (2000).
Lotti, L. et al, “Shc Proteins Are Localized on Endoplasmic Reticulum Membranes and Are Redistributed after Tyrosine Kinase Receptor Activation”, Molec. and Cell. Biol., vol. 16, No. 5, pp. 1946-1954.
Bunney, T. et al, “14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase”, PNAS, vol. 98, No. 7, pp. 4249-5254.
Le, S. et al, “c-Jun N-terminal Kinase Specifically Phoshorylates p66ShcAat Serine 36 in Response to Ultraviolet Irradiation”, J. of Biol. Chem., vol. 276, No. 51, pp. 48332-48336, (2001).
Nemoto, S. et al, Redox Regulation of Forkhead Proteins Through a p66shc-Dependent Signaling Pathway, Science, vol. 295, pp. 2450-2452 (2002).
McClung, J. et al, “Prohibitin:Potential Role in Senescence, Development, and Tumor Suppression”, Exp. Gerontology, vol. 30, No. 2, pp. 99-124 (1995).
Oksvold, M. et al, “Immunocytochemical Localization of Shc and Activated EGF Receptor in Early Endosomes After EGF Stimulation of HeLa Cells”, J. of Histochem CytoChem, vol. 48(1), pp. 21-33 (2000).

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

Protein-protein interactions of p66 ShcA does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Protein-protein interactions of p66 ShcA, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Protein-protein interactions of p66 ShcA will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3643256

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