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RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding

Joris Wauman UGent, Leentje De Ceuninck UGent, Nele Vanderroost UGent, Sam Lievens UGent and Jan Tavernier UGent (2011) JOURNAL OF CELL SCIENCE. 124(6). p.921-932
abstract
Cytokines, such as interferons, erythropoietin, leptin and most interleukins, signal through type 1 cytokine receptors and activate the canonical JAK-STAT pathway. Aberrant cytokine signalling underlies numerous pathologies and adequate, temporary receptor activation is therefore under tight control. Negative-feedback mechanisms are very well studied, but cellular sensitivity also depends on the number of receptors exposed at the cell surface. This is determined by the equilibrium between receptor synthesis and transport to the plasma membrane, internalisation and recycling, degradation and ectodomain shedding, but the molecular basis of how cells establish steady state receptor levels is poorly understood. Here, we report that ring finger protein 41 (RNF41, also known as E3 ubiquitin-protein ligase Nrdp1) interacts with JAK2-associated cytokine receptor complexes and modulates their cell surface exposure and signalling. Moreover, ectopic expression of RNF41 affected turnover of leptin, leukaemia inhibitory factor and interleukin-6 receptor in a dual way: it blocked intracellular cathepsin-L-dependent receptor cleavage and concomitantly enhanced receptor shedding by metalloproteases of the ADAM family. Receptor degradation and shedding are thus interconnected phenomena with a single protein, RNF41, determining the balance.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
MAPPIT, Ectodomain shedding, RNF41, Nrdp1, Type 1 cytokine receptor, ADAM, CELL-SURFACE EXPRESSION, UBIQUITIN LIGASE NRDP1, LEPTIN RECEPTOR, ERYTHROPOIETIN RECEPTOR, PROTEINS, PATHWAY, ENDOCYTOSIS, ACTIVATION, STABILITY, ENZYME, Cathepsin L cleavage
journal title
JOURNAL OF CELL SCIENCE
J. Cell Sci.
volume
124
issue
6
pages
921 - 932
Web of Science type
Article
Web of Science id
000288009900011
JCR category
CELL BIOLOGY
JCR impact factor
6.111 (2011)
JCR rank
38/178 (2011)
JCR quartile
1 (2011)
ISSN
0021-9533
DOI
10.1242/jcs.078055
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1208413
handle
http://hdl.handle.net/1854/LU-1208413
date created
2011-04-13 16:01:58
date last changed
2016-12-19 15:45:16
@article{1208413,
  abstract     = {Cytokines, such as interferons, erythropoietin, leptin and most interleukins, signal through type 1 cytokine receptors and activate the canonical JAK-STAT pathway. Aberrant cytokine signalling underlies numerous pathologies and adequate, temporary receptor activation is therefore under tight control. Negative-feedback mechanisms are very well studied, but cellular sensitivity also depends on the number of receptors exposed at the cell surface. This is determined by the equilibrium between receptor synthesis and transport to the plasma membrane, internalisation and recycling, degradation and ectodomain shedding, but the molecular basis of how cells establish steady state receptor levels is poorly understood. Here, we report that ring finger protein 41 (RNF41, also known as E3 ubiquitin-protein ligase Nrdp1) interacts with JAK2-associated cytokine receptor complexes and modulates their cell surface exposure and signalling. Moreover, ectopic expression of RNF41 affected turnover of leptin, leukaemia inhibitory factor and interleukin-6 receptor in a dual way: it blocked intracellular cathepsin-L-dependent receptor cleavage and concomitantly enhanced receptor shedding by metalloproteases of the ADAM family. Receptor degradation and shedding are thus interconnected phenomena with a single protein, RNF41, determining the balance.},
  author       = {Wauman, Joris and De Ceuninck, Leentje and Vanderroost, Nele and Lievens, Sam and Tavernier, Jan},
  issn         = {0021-9533},
  journal      = {JOURNAL OF CELL SCIENCE},
  keyword      = {MAPPIT,Ectodomain shedding,RNF41,Nrdp1,Type 1 cytokine receptor,ADAM,CELL-SURFACE EXPRESSION,UBIQUITIN LIGASE NRDP1,LEPTIN RECEPTOR,ERYTHROPOIETIN RECEPTOR,PROTEINS,PATHWAY,ENDOCYTOSIS,ACTIVATION,STABILITY,ENZYME,Cathepsin L cleavage},
  language     = {eng},
  number       = {6},
  pages        = {921--932},
  title        = {RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding},
  url          = {http://dx.doi.org/10.1242/jcs.078055},
  volume       = {124},
  year         = {2011},
}

Chicago
Wauman, Joris, Leentje De Ceuninck, Nele Vanderroost, Sam Lievens, and Jan Tavernier. 2011. “RNF41 (Nrdp1) Controls Type 1 Cytokine Receptor Degradation and Ectodomain Shedding.” Journal of Cell Science 124 (6): 921–932.
APA
Wauman, J., De Ceuninck, L., Vanderroost, N., Lievens, S., & Tavernier, J. (2011). RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding. JOURNAL OF CELL SCIENCE, 124(6), 921–932.
Vancouver
1.
Wauman J, De Ceuninck L, Vanderroost N, Lievens S, Tavernier J. RNF41 (Nrdp1) controls type 1 cytokine receptor degradation and ectodomain shedding. JOURNAL OF CELL SCIENCE. 2011;124(6):921–32.
MLA
Wauman, Joris, Leentje De Ceuninck, Nele Vanderroost, et al. “RNF41 (Nrdp1) Controls Type 1 Cytokine Receptor Degradation and Ectodomain Shedding.” JOURNAL OF CELL SCIENCE 124.6 (2011): 921–932. Print.