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van der Geer photo

Peter van der Geer

Assistant Professor
Biochemistry: molecular, biological and biochemical analysis of signal transduction by protein-tyrosine kinases

Office: CSL 322
Office Phone: 619-594-5582
e-mail: pvanderg_at_sciences.sdsu.edu

Curriculum Vita

Fellowships


Research Interests

In a multicellular organism, cells have to communicate with each other so that they can coordinate their activities. Cellular communication is usually mediated by extracellular messenger molecules that are recognized by receptors present on the surface of target cells. Binding of a messenger molecule to a receptor results in biochemical changes within the cell that make it possible for the cell to respond to the incoming message. Many different processes, such as cell division, differentiation, cell migration, metabolism, and cell death, are regulated in response to extracellular messenger molecules.

Signal transduction is the process that translates the binding of a messenger molecule to its receptor into changes in biochemistry, cytoskeletal structure, or gene transcription. Receptor protein-tyrosine kinases represent one class of receptors for extracellular messenger molecules. They contain an extracellular ligand-binding domain and a cytoplasmic protein kinase domain and are activated directly by the interaction with specific extracellular ligands. Activated receptors autophosphorylate on tyrosine residues and autophosphorylation sites act as binding-sites for specific cellular signaling proteins. Signaling proteins, which often contain SH2 or PTB domains, mediate the activation of cellular signal transduction cascades in response to receptor activation.

We are interested in signal transduction by protein-tyrosine kinases with particular emphasis on the role of signaling proteins in this process. Most recently we have focused on proteolytic processing of the CSF-1 receptor and the function of Shc and c-Cbl during protein-tyrosine kinase signaling.


Selected Publications

  1. G. N. Betts, P. van der Geer, and E. A. Komives (2008) Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain. Submitted.
  2. G. Glenn and P. van der Geer (2008) Toll-like receptors stimulate regulated intramembrane proteolysis of the CSF-1 receptor through Erk activation. FEBS Lett. In Press.
  3. G. Glenn and P. van der Geer (2007) CSF-1 and TPA stimulate independent pathways leading to lysosomal degradation or regulated intramembrane proteolysis of the CSF-1 receptor. FEBS Lett. 581, 5377-5381.
  4. S. E. Wiley, M. L. Paddock, E. C. Albresch, L. Gross, P. van der Geer, R. Nechustal, A. N. Murphy, P. A. Jennings, and J. E. Dixon (2007) The outer mitochondrial membrane protein mitoneet contains a novel redox active 2Fe-2S cluster. J. Biol. Chem. 282, 23745-23749.
  5. S. E. Wiley, A. N. Murphy, S. A. Ross, P van der Geer, and J. E. Dixon (2007) MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Proc. Natl. Acad. Sci. USA, 104, 5318-5323.
  6. P. van der Geer and G. Karp (2007) Cell Signaling and Signal Transduction: Communication between cells. Chapter 16 in: Cell and Molecular Biology 5th edition. J. Wiley and Sons Inc. New York.
  7. J. Meisenhelder and P. van der Geer. (2006) Phosphopeptide Mapping: A basic Protocol. in: Cell Biology. Elsevier Science USA.
  8. J. R. MacFayden, O. Hayworth, D. Robertson, D. Hardie, M.-T. Webster, H. R. Morris, M. Panico, M. Sutton-Smith, A. Dell, P. van der Geer, D. Wienke, C. Buckley and C. Isacke (2005) Endosialin (TEM1, CD248) is a marker of stromal fibroblasts and is not selectively expressed on tumor endothelium. FEBS Lett. 579, 2569-2575.
  9. J. Copp, S. Wiley, M. W. Ward and P. van der Geer (2005) Hypertonic shock inhibits growth factor signaling, induces caspase 3 activation, and causes reversible fragmentation of the mitochondrial network. Am. J. Phys. Cell Physiol. C403-415.
  10. K. Wilhelmsen, J. Copp, G. Glenn, R. Hoffmann, P. Tucker and P. van der Geer. (2004) Purification and identification of protein-tyrosine kinase-binding proteins using synthetic phosphopeptides as affinity reagents. Mol. Cell. Proteomics 3, 887-895.
  11. G. Glenn and P. van der Geer (2004) Ripping of receptor protein-tyrosine kinases, a new development in signal transduction. Recent Res. Devel. Mol. Cell. Biol. 5, 113-133.

Copyright © 2008. All rights reserved. Web editor: A. L. Cooksy. Page last modified: Thu 14 Feb 2008 05:02:06.