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Protein tyrosine kinase PYK2 involved in Ca2+-induced regulation of ion channel and MAP kinase functions
PYK2 activation may provide a mechanism for a variety of short- and long-term calcium-dependent signalling events in the nervous system.
A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
It is proposed that Pyk2 acts with Src to link Gi- and Gq-coupled receptors with Grb2 and Sos to activate the MAP kinase signalling pathway in PC12 cells.
RNA interference screen for human genes associated with West Nile virus infection
This study provides a comprehensive molecular portrait of WNV–human cell interactions that forms a model for understanding single plus-stranded RNA virus infection, and reveals potential antiviral targets.
Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport.
- Diego Peretti, Nili Dahan, E. Shimoni, K. Hirschberg, S. Lev
- BiologyMolecular biology of the cell
- 1 September 2008
It is shown that the integral ER-membrane proteins V AP-A and VAP-B affect the structural and functional integrity of the Golgi complex, and this work proposes that Nir2, OSBP, and CERT function coordinately at the ER-Golgi membrane contact sites, thereby affecting the lipid composition of the golgi membranes and consequently their structural andfunctional identities.
The VAP protein family: from cellular functions to motor neuron disease.
Activation of Pyk2 by Stress Signals and Coupling with JNK Signaling Pathway
The tyrosine kinase Pyk2 represents a cell type-specific, stress-sensitive mediator of the JNK signaling pathway and was activated by tumor necrosis factor α, by ultraviolet irradiation, and by changes in osmolarity.
Differential Regulation of Endoplasmic Reticulum Structure through VAP-Nir Protein Interaction*
- Roy Amarilio, Sree Ramachandran, H. Sabanay, S. Lev
- Biology, ChemistryJournal of Biological Chemistry
- 18 February 2005
The integral ER-membrane protein VAP-B causes a striking rearrangement of the ER through interaction with the Nir2 and Nir3 proteins, demonstrating new mechanisms for the regulation of ER structure.
Non-vesicular lipid transport by lipid-transfer proteins and beyond
- S. Lev
- BiologyNature Reviews Molecular Cell Biology
- 1 October 2010
Understanding the mechanisms by which lipids are transported and distributed between cellular membranes, and elucidating the role of LTPs in intracellular lipid transport and homeostasis, are currently subjects of intensive study.
Tethering the assembly of SNARE complexes.
Identification of a Novel Family of Targets of PYK2 Related to Drosophila Retinal Degeneration B (rdgB) Protein
- S. Lev, J. Hernandez, R. Martinez, Alon Chen, G. Plowman, J. Schlessinger
- BiologyMolecular and Cellular Biology
- 1 March 1999
It is proposed that the Nir and rdgB proteins represent a new family of evolutionarily conserved PYK2-binding proteins that play a role in the control of calcium and phosphoinositide metabolism downstream of G-protein-coupled receptors.