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The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases

Kitching, Richard; Wong, Michael J; Koehler, David; Burger, Angelika M; Landberg, Göran LU ; Gish, Gerald and Seth, Arun (2003) In Biochimica et Biophysica Acta 1639(2). p.104-112
Abstract
A breast cancer-associated mRNA originally cloned as a 475-bp partial cDNA from a library enriched for tumour cDNAs [Oncogene 16 (1998) 327] is expressed at high levels in breast and prostate cancer cells. Immunohistochemical analysis indicates that the protein is expressed in primary breast tumours. We used RT-PCR to generate a full-length 2852 nt mRNA sequence that includes the hypothetical open reading frame (ORF) for human RNF11. Our analysis shows that RNF11 encodes modular domains and motifs likely to interact with other proteins involved in oncogenesis. Chief among these are the RING-H2 finger domain that could facilitate the degradation of specific substrate(s) involved in oncogenesis and the PY motif which binds to WW-domain... (More)
A breast cancer-associated mRNA originally cloned as a 475-bp partial cDNA from a library enriched for tumour cDNAs [Oncogene 16 (1998) 327] is expressed at high levels in breast and prostate cancer cells. Immunohistochemical analysis indicates that the protein is expressed in primary breast tumours. We used RT-PCR to generate a full-length 2852 nt mRNA sequence that includes the hypothetical open reading frame (ORF) for human RNF11. Our analysis shows that RNF11 encodes modular domains and motifs likely to interact with other proteins involved in oncogenesis. Chief among these are the RING-H2 finger domain that could facilitate the degradation of specific substrate(s) involved in oncogenesis and the PY motif which binds to WW-domain proteins, several of which are known to be E3 ubiquitin ligases. Our GST-pulldown and immunoprecipitation results indicate that RNF11 interacts with the E3 ligase AIP4 when coexpressed with RNF11 in mammalian cells. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochimica et Biophysica Acta
volume
1639
issue
2
pages
104 - 112
publisher
Elsevier
external identifiers
  • pmid:14559117
  • scopus:1642414402
ISSN
0006-3002
DOI
language
English
LU publication?
no
id
1c7227db-cc54-41b8-b75e-cbb004a2594f (old id 1127179)
date added to LUP
2008-06-10 09:04:19
date last changed
2018-05-29 10:30:29
@article{1c7227db-cc54-41b8-b75e-cbb004a2594f,
  abstract     = {A breast cancer-associated mRNA originally cloned as a 475-bp partial cDNA from a library enriched for tumour cDNAs [Oncogene 16 (1998) 327] is expressed at high levels in breast and prostate cancer cells. Immunohistochemical analysis indicates that the protein is expressed in primary breast tumours. We used RT-PCR to generate a full-length 2852 nt mRNA sequence that includes the hypothetical open reading frame (ORF) for human RNF11. Our analysis shows that RNF11 encodes modular domains and motifs likely to interact with other proteins involved in oncogenesis. Chief among these are the RING-H2 finger domain that could facilitate the degradation of specific substrate(s) involved in oncogenesis and the PY motif which binds to WW-domain proteins, several of which are known to be E3 ubiquitin ligases. Our GST-pulldown and immunoprecipitation results indicate that RNF11 interacts with the E3 ligase AIP4 when coexpressed with RNF11 in mammalian cells.},
  author       = {Kitching, Richard and Wong, Michael J and Koehler, David and Burger, Angelika M and Landberg, Göran and Gish, Gerald and Seth, Arun},
  issn         = {0006-3002},
  language     = {eng},
  number       = {2},
  pages        = {104--112},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases},
  url          = {http://dx.doi.org/},
  volume       = {1639},
  year         = {2003},
}