The Neuronal Rho-GEF Kalirin-7 Interacts with PDZ Domain–Containing Proteins and Regulates Dendritic Morphogenesis
@article{Penzes2001TheNR, title={The Neuronal Rho-GEF Kalirin-7 Interacts with PDZ Domain–Containing Proteins and Regulates Dendritic Morphogenesis}, author={Peter Penzes and Richard C. Johnson and Rita Sattler and Xiaoqun Zhang and Richard L. Huganir and Vikram Kambampati and Richard E. Mains and Betty A. Eipper}, journal={Neuron}, year={2001}, volume={29}, pages={229-242} }
Figures and Tables from this paper
400 Citations
Distinct Roles for the Two Rho GDP/GTP Exchange Factor Domains of Kalirin in Regulation of Neurite Growth and Neuronal Morphology
- BiologyThe Journal of Neuroscience
- 2001
The actin cytoskeleton, essential for neuronal development, is regulated in part by small GTP binding proteins of the Rho subfamily, and Kalirin-9 overexpression in cultured cortical neurons induces longer neurites and altered neuronal morphology.
Scaffold Protein X11α Interacts with Kalirin-7 in Dendrites and Recruits It to Golgi Outposts*
- BiologyThe Journal of Biological Chemistry
- 2014
It is shown that kalirin-7 and X11α form a complex in the brain, and this interaction is mediated by the C terminus of kal Kirin-7, a critical regulator of dendritic spine remodeling.
Preso, A Novel PSD-95-Interacting FERM and PDZ Domain Protein That Regulates Dendritic Spine Morphogenesis
- BiologyThe Journal of Neuroscience
- 2008
It is suggested that Preso positively regulates spine density through its interaction with the synaptic plasma membrane, actin filaments, PSD-95, and the βPix-based Rac1 signaling pathway.
Kalirin-7 Is an Essential Component of both Shaft and Spine Excitatory Synapses in Hippocampal Interneurons
- BiologyThe Journal of Neuroscience
- 2008
Overexpression of Kal7 increases dendritic branching, inducing formation of spine-like structures along the dendrites and on the soma of normally aspiny hippocampal interneurons, and joins Shank3 and GluR2 as molecules with a level of expression at excitatory synapses that titrates the number of dendrite spines.
Kalirin-7 Is Required for Synaptic Structure and Function
- Biology, PsychologyThe Journal of Neuroscience
- 2008
In vitro studies demonstrated that overexpression of Kal7 increased dendritic spine density, whereas reduced expression of endogenous Kal7 decreased spinedensity, and Expression of exogenous Kal7 in Kal7KO neurons rescued this deficit.
Kalirin: A Dual Rho Guanine Nucleotide Exchange Factor That Is So Much More Than the Sum of Its Many Parts
- BiologyThe Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry
- 2005
Kalirin is a large neuronal dual Rho GEF that activates Rac1, RhoA, and RhoG via its two RhoGEF domains, and this alternatively spliced gene generates developmentally regulated transcripts that yield proteins localized to the postsynaptic density (PSD).
Autonomous functions for the Sec14p/spectrin-repeat region of Kalirin.
- BiologyExperimental cell research
- 2008
Kalirin Binds the NR2B Subunit of the NMDA Receptor, Altering Its Synaptic Localization and Function
- BiologyThe Journal of Neuroscience
- 2011
A novel and functionally important interaction between the NR2B subunit of the NMDA receptor and Kalirin, proteins known to be essential for normal synaptic plasticity are demonstrated.
References
SHOWING 1-10 OF 126 REFERENCES
An Isoform of Kalirin, a Brain-specific GDP/GTP Exchange Factor, Is Enriched in the Postsynaptic Density Fraction*
- BiologyThe Journal of Biological Chemistry
- 2000
Kalirin-7 is the first guanine-nucleotide exchange factor identified in the postsynaptic density, where it is positioned optimally to regulate signal transduction pathways connecting membrane proteins and the actin cytoskeleton.
UNC-73 Activates the Rac GTPase and Is Required for Cell and Growth Cone Migrations in C. elegans
- BiologyCell
- 1998
Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin
- Biology, ChemistryThe Journal of Neuroscience
- 1998
The results indicate that the actin-mediated stability of synaptic structure is disrupted by intense glutamate receptor activity and that calcineurin blockers may be useful in preventing such destabilization.
Glutamate Receptor Anchoring Proteins and the Molecular Organization of Excitatory Synapses
- Biology, ChemistryAnnals of the New York Academy of Sciences
- 1999
The cytoplasmic C‐terminal tail of certain glutamate receptor subunits interact with specific PDZ domain‐containing proteins, which may underlie the clustering, targeting, and immobilization of the glutamate receptors at postsynaptic sites.
Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1997
It is proposed that spinophilin represents a novel targeting subunit for PP1, which directs the enzyme to those substrates in the dendritic spine compartment, e.g., neurotransmitter receptors, which mediate the regulation of synaptic function by PP1.
Regulation of Dendritic Growth and Remodeling by Rho, Rac, and Cdc42
- BiologyNeuron
- 1997
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
- BiologyScience
- 1995
The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses.
Kalirin, a Multifunctional PAM COOH-terminal Domain Interactor Protein, Affects Cytoskeletal Organization and ACTH Secretion from AtT-20 Cells*
- BiologyThe Journal of Biological Chemistry
- 1999
Peptidylglycine α-amidating monooxygenase (PAM), an enzyme essential for biosynthesis of many peptides, is an integral membrane protein with trafficking information in both its lumenal and cytosol domains, and the PAM-Kalirin interaction may coordinate intragranular with cytosolic events.