Abstract:
:Analysis of the fate of the p185HER2 oncoprotein following activation by heregulin beta1 revealed the induction of the tyrosine-phosphorylation, down-modulation, and polyubiquitination of p185HER2. Receptor ubiquitination was suppressed in cells treated with heregulin beta1 in the presence of sodium azide, an inhibitor of ATP-dependent reactions, or genistein, a tyrosine kinase protein inhibitor, indicating the requirement for kinase activity and ATP in p185HER2 polyubiquitination. Ubiquitinated p185HER2 was degradated by the 26S proteasome proteolytic pathway. Kinetics and inhibition experiments indicated that endocytosis of the receptor occurs downstream of the initiation of the degradation process.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Magnifico A,Tagliabue E,Ardini E,Casalini P,Colnaghi MI,Ménard Sdoi
10.1016/s0014-5793(97)01612-8subject
Has Abstractpub_date
1998-01-30 00:00:00pages
129-31issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01612-8journal_volume
422pub_type
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