JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mori, S.
Right arrow Articles by Heldin, C. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mori, S.
Right arrow Articles by Heldin, C. H.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 269, Issue 7, 4917-4921, 02, 1994

A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor beta-receptor is critical for ligand-mediated endocytosis

S Mori, L Ronnstrand, L Claesson-Welsh and CH Heldin
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.

The importance of tyrosine residues in ligand-mediated endocytosis of the platelet-derived growth factor beta-receptor was analyzed using a series of tyrosine residue-mutated beta-receptors, which together cover all of the tyrosine residues in the juxtamembrane segment, the kinase insert, and the carboxyl-terminal tail; also certain of the tyrosine residues within the first and second parts of the kinase domain were examined. Of all of these tyrosine residues, only Tyr-579 seemed to be important for internalization, since mutation of this residue resulted in substantial reduction in the rate of ligand-induced receptor internalization (approximately 60% of the wild-type level). Replacement of Tyr-579 by either an aromatic (Phe) or a nonaromatic (Asp) residue reduced the efficiency of the mutant receptors in internalization to the same extent, suggesting that the role of Tyr-579 in the beta- receptor is different from that of the previously described tyrosine- based internalization motifs, which were first determined for the low density lipoprotein receptor. Tyr-579 has been found to be an autophosphorylation site in the beta-receptor. Moreover, the internalization rate of a kinase negative receptor mutant was not altered by the additional mutation of Tyr-579. Thus, it is likely that phosphorylation of Tyr-579 is important for ligand-induced internalization of the beta-receptor.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
A. De Donatis, G. Comito, F. Buricchi, M. C. Vinci, A. Parenti, A. Caselli, G. Camici, G. Manao, G. Ramponi, and P. Cirri
Proliferation Versus Migration in Platelet-derived Growth Factor Signaling: THE KEY ROLE OF ENDOCYTOSIS
J. Biol. Chem., July 18, 2008; 283(29): 19948 - 19956.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Franco, O. Furstoss, V. Simon, C. Benistant, W. J. Hong, and S. Roche
The Adaptor Protein Tom1L1 Is a Negative Regulator of Src Mitogenic Signaling Induced by Growth Factors.
Mol. Cell. Biol., March 1, 2006; 26(5): 1932 - 1947.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
H. Wu, D. A. Windmiller, L. Wang, and J. M. Backer
YXXM Motifs in the PDGF-{beta} Receptor Serve Dual Roles as Phosphoinositide 3-Kinase Binding Motifs and Tyrosine-based Endocytic Sorting Signals
J. Biol. Chem., October 17, 2003; 278(42): 40425 - 40428.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. Voytyuk, J. Lennartsson, A. Mogi, G. Caruana, S. Courtneidge, L. K. Ashman, and L. Ronnstrand
Src Family Kinases Are Involved in the Differential Signaling from Two Splice Forms of c-Kit
J. Biol. Chem., March 7, 2003; 278(11): 9159 - 9166.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Hackzell, H. Uramoto, H. Izumi, K. Kohno, and K. Funa
p73 Independent of c-Myc Represses Transcription of Platelet-derived Growth Factor beta -Receptor through Interaction with NF-Y
J. Biol. Chem., October 11, 2002; 277(42): 39769 - 39776.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Sorkina, F. Huang, L. Beguinot, and A. Sorkin
Effect of Tyrosine Kinase Inhibitors on Clathrin-coated Pit Recruitment and Internalization of Epidermal Growth Factor Receptor
J. Biol. Chem., July 19, 2002; 277(30): 27433 - 27441.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
P. Chiarugi, P. Cirri, M. L. Taddei, D. Talini, L. Doria, T. Fiaschi, F. Buricchi, E. Giannoni, G. Camici, G. Raugei, et al.
New perspectives in PDGF receptor downregulation: the main role of phosphotyrosine phosphatases
J. Cell Sci., May 15, 2002; 115(10): 2219 - 2232.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
H Izumi, C Molander, L. Penn, A Ishisaki, K Kohno, and K Funa
Mechanism for the transcriptional repression by c-Myc on PDGF (&bgr;)-receptor
J. Cell Sci., January 4, 2001; 114(8): 1533 - 1544.
[Abstract] [PDF]


Home page
Physiol. Rev.Home page
C.-H. Heldin and B. Westermark
Mechanism of Action and In Vivo Role of Platelet-Derived Growth Factor
Physiol Rev, October 1, 1999; 79(4): 1283 - 1316.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Matsumoto, K. Yokote, K. Tamura, M. Takemoto, H. Ueno, Y. Saito, and S. Mori
Platelet-derived Growth Factor Activates p38 Mitogen-activated Protein Kinase through a Ras-dependent Pathway That Is Important for Actin Reorganization and Cell Migration
J. Biol. Chem., May 14, 1999; 274(20): 13954 - 13960.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
G. Strous and R Govers
The ubiquitin-proteasome system and endocytosis
J. Cell Sci., January 5, 1999; 112(10): 1417 - 1423.
[Abstract] [PDF]


Home page
J. Pharmacol. Exp. Ther.Home page
D. E. Brenneman, J. Hauser, E. Neale, S. Rubinraut, M. Fridkin, A. Davidson, and I. Gozes
Activity-Dependent Neurotrophic Factor: Structure-Activity Relationships of Femtomolar-Acting Peptides
J. Pharmacol. Exp. Ther., May 1, 1998; 285(2): 619 - 627.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J. L. Gommerman, R. Rottapel, and S. A. Berger
Phosphatidylinositol 3-Kinase and Ca2+ Influx Dependence for Ligand-stimulated Internalization of the c-Kit Receptor
J. Biol. Chem., November 28, 1997; 272(48): 30519 - 30525.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Hamer, C. R. Haft, J.-P. Paccaud, C. Maeder, S. Taylor, and J.-L. Carpentier
Dual Role of a Dileucine Motif in Insulin Receptor Endocytosis
J. Biol. Chem., August 29, 1997; 272(35): 21685 - 21691.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Yokote, B. Margolis, C.-H. Heldin, and L. Claesson-Welsh
Grb7 is a Downstream Signaling Component of Platelet-derived Growth Factor alpha - and beta -Receptors
J. Biol. Chem., November 29, 1996; 271(48): 30942 - 30949.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Mori, K. Tanaka, S. Omura, and Y. Saito
Degradation Process of Ligand-stimulated Platelet-derived Growth Factor beta-Receptor Involves Ubiquitin-Proteasome Proteolytic Pathway
J. Biol. Chem., December 8, 1995; 270(49): 29447 - 29452.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Joly, A. Kazlauskas, and S. Corvera
Phosphatidylinositol 3-Kinase Activity Is Required at a Postendocytic Step in Platelet-derived Growth Factor Receptor Trafficking
J. Biol. Chem., June 2, 1995; 270(22): 13225 - 13230.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1994 by the American Society for Biochemistry and Molecular Biology.