ArticleExperimental cell research2008
Autonomous functions for the Sec14p/spectrin-repeat region of Kalirin.
Article in Experimental cell research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 34 citations in OpenAlex.
- Identification and characterization of human KALRN mRNA and Kalirin protein isoforms.Cerebral cortex (New York, N.Y. : 1991) · 2024Article
- Autoinhibition of the GEF activity of cytoskeletal regulatory protein Trio is disrupted in neurodevelopmental disorder-related genetic variants.The Journal of biological chemistry · 2022Article
- Differential Effects of Sevoflurane Exposure on Long-Term Fear Memory in Neonatal and Adult Rats.Molecular neurobiology · 2022Article
- Review
- Trio family proteins as regulators of cell migration and morphogenesis in development and disease - mechanisms and cellular contexts.Journal of cell science · 2021Review
- Review
- Lipid transfer proteins and instructive regulation of lipid kinase activities: Implications for inositol lipid signaling and disease.Advances in biological regulation · 2020Review
- Neurodevelopmental disease-associated de novo mutations and rare sequence variants affect TRIO GDP/GTP exchange factor activity.Human molecular genetics · 2017Article
- Kalirin is required for BDNF-TrkB stimulated neurite outgrowth and branching.Neuropharmacology · 2016Article
- Exome sequencing discloses KALRN homozygous variant as likely cause of intellectual disability and short stature in a consanguineous pedigree.Human genomics · 2016Article
- Kalirin-9 and Kalirin-12 Play Essential Roles in Dendritic Outgrowth and Branching.Cerebral cortex (New York, N.Y. : 1991) · 2015Article
- An N-terminal Amphipathic Helix Binds Phosphoinositides and Enhances Kalirin Sec14 Domain-mediated Membrane Interactions.The Journal of biological chemistry · 2015Article
- Nonenzymatic domains of Kalirin7 contribute to spine morphogenesis through interactions with phosphoinositides and Abl.Molecular biology of the cell · 2014Article
- Neuronal Rho GEFs in synaptic physiology and behavior.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2013Review
- Kalrn plays key roles within and outside of the nervous system.BMC neuroscience · 2012Article
- Mechanisms of psychostimulant-induced structural plasticity.Cold Spring Harbor perspectives in medicine · 2012Article
- Structural organization of the nine spectrin repeats of Kalirin.Biochemistry · 2012Article
- High-throughput single-cell manipulation in brain tissue.PloS one · 2012Article
- Article
- Kalirin-7 is necessary for normal NMDA receptor-dependent synaptic plasticity.BMC neuroscience · 2011Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Kalirin is a GDP/GTP exchange factor (GEF) for Rho proteins that modulates the actin cytoskeleton in neurons. Alternative splicing generates Delta-isoforms, which encode the RhoGEF domain, but lack the N-terminal Sec14p domain and first 4 spectrin-like repeats of the full-length isoforms. Splicing has functional consequences, with Kal7 but not DeltaKal7 causing formation of dendritic spines. Cells lacking endogenous Kalirin were used to explore differences between these splice variants. Expression of DeltaKal7 in this system induces extensive lamellipodial sheets, while expression of Kal7 induces formation of adherent compact, round cells with abundant cortical actin. Based on in vitro and cell-based assays, Kal7 and DeltaKal7 are equally active GEFs, suggesting that other domains are involved in controlling cell morphology. Catalytically inactive Kal7 and a Kalirin fragment which includes only Sec14p and spectrin-like domains retain the ability to produce compact, round cells and fractionate as high molecular weight complexes. Separating the Sec14p domain from the spectrin-like repeats eliminates the ability of Kal7 to cause this response. The isolated Sec14p domain binds PI(3,5)P2 and PI3P, but does not alter cell morphology. We conclude that the Sec14p and N-terminal spectrin-like domains of Kalirin play critical roles in distinguishing the actions of full-length and Delta-Kalirin proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.