Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print January 5, 2005
Mol. Biol. Cell 10.1091/mbc.E04-09-0832

A more recent version of this article appeared on March 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E04-09-0832v1
16/3/1268    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Huang, F.
Right arrow Articles by Sorkin, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, F.
Right arrow Articles by Sorkin, A.

Submitted on September 23, 2004
Revised on December 14, 2004
Accepted on December 22, 2004

Grb2-mediated Recruitment of the RING Domain of Cbl to the EGF Receptor Is Essential and Sufficient to Support Receptor Endocytosis

Fangtian Huang and Alexander Sorkin*

Department of Pharmacology, University of Colorado Health Sciences Center, Aurora, CO 80045

Monitoring Editor: Sandra Schmid

Knock-down of Grb2 by RNA interference (RNAi) strongly inhibits clathrin-mediated endocytosis of the EGF receptor (EGFR). To gain insights into the function of Grb2 in EGFR endocytosis, we have generated cell lines in which endogenous Grb2 was replaced by YFP-tagged Grb2 expressed at the physiological level. In these cells Grb2-YFP fully reversed the inhibitory effect of Grb2 knock-down on EGFR endocytosis and moreover, trafficked together with EGFR during endocytosis. Overexpression of Grb2-binding protein, c-Cbl did not restore endocytosis in Grb2-depleted cells. However, EGFR endocytosis was rescued in Grb2-depleted cells by chimeric proteins consisting of the Src Homology (SH) 2 domain of Grb2 fused to c-Cbl. The "knock-down and rescue" analysis revealed that the expression of Cbl-Grb2/SH2 fusions containing RING finger domain of Cbl restores normal ubiquitylation and internalization of the EGFR in the absence of Grb2, consistent with the important role of the RING domain in EGFR endocytosis. In contrast, the carboxyl-terminal domain of Cbl, when attached to Grb2 SH2 domain, had 4-times smaller endocytosis-rescue effect as compared with the RING-containing chimeras. Taken together, the data suggest that the interaction of Cbl carboxyl-terminus with CIN85 has a minor and a redundant role in EGFR internalization. We concluded that Grb2-mediated recruitment of the functional RING domain of Cbl to the EGFR is essential and sufficient to support receptor endocytosis.

*Corresponding author. E-mail: alexander.sorkin{at}uchsc.edu




This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
S. Pennock and Z. Wang
A Tale of Two Cbls: Interplay of c-Cbl and Cbl-b in Epidermal Growth Factor Receptor Downregulation
Mol. Cell. Biol., May 1, 2008; 28(9): 3020 - 3037.
[Abstract] [Full Text] [PDF]

Home page
 Mol Cancer ResHome page
N. M. Pedersen, I. H. Madshus, C. Haslekas, and E. Stang
Geldanamycin-Induced Down-Regulation of ErbB2 from the Plasma Membrane Is Clathrin Dependent but Proteasomal Activity Independent
Mol. Cancer Res., March 1, 2008; 6(3): 491 - 500.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
E. M. Khan, R. Lanir, A. R. Danielson, and T. Goldkorn
Epidermal growth factor receptor exposed to cigarette smoke is aberrantly activated and undergoes perinuclear trafficking
FASEB J, March 1, 2008; 22(3): 910 - 917.
[Abstract] [Full Text] [PDF]

Home page
 CarcinogenesisHome page
A. J. Galliher-Beckley and W. P. Schiemann
Grb2 binding to Tyr284 in T{beta}R-II is essential for mammary tumor growth and metastasis stimulated by TGF-{beta}
Carcinogenesis, February 1, 2008; 29(2): 244 - 251.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
E. Giurisato, M. Cella, T. Takai, T. Kurosaki, Y. Feng, G. D. Longmore, M. Colonna, and A. S. Shaw
Phosphatidylinositol 3-Kinase Activation Is Required To Form the NKG2D Immunological Synapse
Mol. Cell. Biol., December 15, 2007; 27(24): 8583 - 8599.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
F. Huang, L. K. Goh, and A. Sorkin
EGF receptor ubiquitination is not necessary for its internalization
PNAS, October 23, 2007; 104(43): 16904 - 16909.
[Abstract] [Full Text] [PDF]

Home page
 CarcinogenesisHome page
M. V. Grandal, R. Zandi, M. W. Pedersen, B. M. Willumsen, B. van Deurs, and H. S. Poulsen
EGFRvIII escapes down-regulation due to impaired internalization and sorting to lysosomes
Carcinogenesis, July 1, 2007; 28(7): 1408 - 1417.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Li, M. Lorinczi, K. Ireton, and L. A. Elferink
Specific Grb2-mediated Interactions Regulate Clathrin-dependent Endocytosis of the cMet-tyrosine Kinase
J. Biol. Chem., June 8, 2007; 282(23): 16764 - 16775.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Interv.Home page
M. Miranda and A. Sorkin
Regulation of Receptors and Transporters by Ubiquitination: New Insights into Surprisingly Similar Mechanisms
Mol. Interv., June 1, 2007; 7(3): 157 - 167.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
K. A. Stern, G. D. Visser Smit, T. L. Place, S. Winistorfer, R. C. Piper, and N. L. Lill
Epidermal Growth Factor Receptor Fate Is Controlled by Hrs Tyrosine Phosphorylation Sites That Regulate Hrs Degradation
Mol. Cell. Biol., February 1, 2007; 27(3): 888 - 898.
[Abstract] [Full Text] [PDF]

Home page
 J Mol EndocrinolHome page
L. Bonaccorsi, D. Nosi, M. Muratori, L. Formigli, G. Forti, and E. Baldi
Altered endocytosis of epidermal growth factor receptor in androgen receptor positive prostate cancer cell lines
J. Mol. Endocrinol., January 1, 2007; 38(1): 51 - 66.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
S. E. Gustin, C. B. F. Thien, and W. Y. Langdon
Cbl-b Is a Negative Regulator of Inflammatory Cytokines Produced by IgE-Activated Mast Cells
J. Immunol., November 1, 2006; 177(9): 5980 - 5989.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Tanos and A. M. Pendergast
Abl Tyrosine Kinase Regulates Endocytosis of the Epidermal Growth Factor Receptor
J. Biol. Chem., October 27, 2006; 281(43): 32714 - 32723.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
C. V. Garat, D. Fankell, P. F. Erickson, J. E.-B. Reusch, N. N. Bauer, I. F. McMurtry, and D. J. Klemm
Platelet-Derived Growth Factor BB Induces Nuclear Export and Proteasomal Degradation of CREB via Phosphatidylinositol 3-Kinase/Akt Signaling in Pulmonary Artery Smooth Muscle Cells.
Mol. Cell. Biol., July 1, 2006; 26(13): 4934 - 4948.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. M. Khan, J. M. Heidinger, M. Levy, M. P. Lisanti, T. Ravid, and T. Goldkorn
Epidermal Growth Factor Receptor Exposed to Oxidative Stress Undergoes Src- and Caveolin-1-dependent Perinuclear Trafficking
J. Biol. Chem., May 19, 2006; 281(20): 14486 - 14493.
[Abstract] [Full Text] [PDF]

Home page
 Circ. Res.Home page
S. Mukherjee, M. Tessema, and A. Wandinger-Ness
Vesicular Trafficking of Tyrosine Kinase Receptors and Associated Proteins in the Regulation of Signaling and Vascular Function
Circ. Res., March 31, 2006; 98(6): 743 - 756.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
L. E. Johannessen, N. M. Pedersen, K. W. Pedersen, I. H. Madshus, and E. Stang
Activation of the epidermal growth factor (EGF) receptor induces formation of EGF receptor- and Grb2-containing clathrin-coated pits.
Mol. Cell. Biol., January 1, 2006; 26(2): 389 - 401.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.