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001-es BibID:BIBFORM004832
035-os BibID:(scopus)12144266330 (wos)000225455700015
Első szerző:Citri, Ami
Cím:Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation / Citri, A., Gan, J., Mosesson, Y., Vereb, G., Szollosi, J., Yarden, Y.
Dátum:2004
Megjegyzések:ErbB-2/HER2 is an oncogenic tyrosine kinase that regulates a signalling network by forming ligand-induced heterodimers with several growth factor receptors of the ErbB family. Hsp90 and co-chaperones regulate degradation of ErbB-2 but not other ErbB members. Here, we report that the role of Hsp90 in modulating the ErbB network extends beyond regulation of protein stability. The capacity of ErbB-2 to recruit ligand-bound receptors into active heterodimers is limited by Hsp90, which is dissociated from ErbB-2 following ligand-induced heterodimerization. We show that Hsp90 binds a specific loop within the kinase domain of ErbB-2, thereby restraining heterodimer formation and catalytic function. These results define a role for Hsp90 as a molecular switch regulating the ErbB signalling network by limiting formation of ErbB-2-centred receptor complexes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Amino Acid Motifs
Amino Acid Sequence
Dimerization
HSP90 Heat-Shock Proteins
metabolism
Molecular Sequence Data
physiology
Proteins
Receptor,erbB-2
Research
Signal Transduction
Support
Megjelenés:EMBO Reports. - 5 : 12 (2004), p. 1165-1170. -
További szerzők:Gan, Judith Mosesson, Yaron Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Yarden, Yosef
Internet cím:elektronikus változat
DOI
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2.

001-es BibID:BIBFORM004734
Első szerző:Mosesson, Yaron
Cím:Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation / Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J., Yarden, Y.
Dátum:2003
ISSN:021-9258 (Print)
Megjegyzések:Growth factors stimulate specific receptor tyrosine kinases, but subsequent receptor endocytosis terminates signaling. The ubiquitin ligase c-Cbl targets epidermal growth factor receptors (EGFRs) to endocytosis by tagging them with multiple ubiquitin molecules. However, the type of ubiquitylation is unknown; whereas polyubiquitin chains signal proteasomal degradation, ubiquitin monomers control other processes. We report that in isolation c-Cbl mediates monoubiquitylation rather than polyubiquitylation of EGFRs. Consistent with the sufficiency of monoubiquitylation, when fused to the tail of EGFR, a single ubiquitin induces receptor endocytosis and degradation in cells. By using receptor and ubiquitin mutants, we infer that c-Cbl attaches a founder monoubiquitin to the kinase domain of EGFR and this is complemented by the conjugation of additional monoubiquitins. Hence, receptor tyrosine kinases are desensitized through conjugation of multiple monoubiquitins, which is distinct from polyubiquitin-dependent proteasomal degradation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animals
Cells
chemistry
Cho Cells
Cricetinae
Electrophoresis,Polyacrylamide Gel
Endocytosis
Epidermal Growth Factor
Genetic Vectors
Immunoblotting
Ligases
metabolism
Mice
Microscopy,Fluorescence
Plasmids
Precipitin Tests
Protein Structure,Tertiary
Protein-Tyrosine Kinases
Proteins
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-cbl
Receptor Protein-Tyrosine Kinases
Research
Support
Time Factors
Transfection
Ubiquitin
Ubiquitin-Protein Ligases
Megjelenés:The Journal of Biological Chemistry. - 278 : 24 (2003), p. 21323-21326. -
További szerzők:Shtiegman, K. Katz, M. Zwang, Y. Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Yarden, Yosef
Internet cím:elektronikus változat
elektronikus változat
DOI
Borító:
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