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The molecular mechanism underlying long-term potentiation (LTP) is critical for understanding learning and memory. CaMKII, a key kinase involved in LTP, is both necessary and sufficient for LTP induction. However, how CaMKII gives rise to LTP is currently unknown. Recent studies suggest that Rho GTPases are necessary for LTP. Rho GTPases are activated by Rho guanine exchange factors (RhoGEFs), but the RhoGEF(s) required for LTP also remain unknown. Here, using a combination of molecular, electrophysiological, and imaging techniques, we show that the RhoGEF Kalirin and its paralog Trio play critical and redundant roles in excitatory synapse structure and function. Furthermore, we show that CaMKII phosphorylation of Kalirin is sufficient to enhance synaptic AMPA receptor expression, and that preventing CaMKII signaling through Kalirin and Trio prevents LTP induction. Thus, our data identify Kalirin and Trio as the elusive targets of CaMKII phosphorylation responsible for AMPA receptor up-regulation during LTP.

Titel:	Kalirin and Trio proteins serve critical roles in excitatory synaptic transmission and LTP.
Autor/in / Beteiligte Person:	Herring, BE ; Nicoll, RA
Link:	Full Text Finder (Volltext)
Zeitschrift:	Proceedings of the National Academy of Sciences of the United States of America, Jg. 113 (2016-02-23), Heft 8, S. 2264-9
Veröffentlichung:	Washington, DC : National Academy of Sciences, 2016
Medientyp:	academicJournal
ISSN:	1091-6490 (electronic)
DOI:	10.1073/pnas.1600179113
Schlagwort:	Animals CA1 Region, Hippocampal physiology Calcium-Calmodulin-Dependent Protein Kinase Type 2 metabolism Gene Knockdown Techniques Gene Knockout Techniques Guanine Nucleotide Exchange Factors antagonists & inhibitors Guanine Nucleotide Exchange Factors genetics HEK293 Cells Humans In Vitro Techniques Mice Models, Neurological Nerve Tissue Proteins antagonists & inhibitors Nerve Tissue Proteins genetics Phosphoproteins antagonists & inhibitors Phosphoproteins genetics Phosphoproteins physiology Phosphorylation Protein Serine-Threonine Kinases antagonists & inhibitors Protein Serine-Threonine Kinases genetics Protein Serine-Threonine Kinases physiology Rats Receptors, AMPA metabolism Receptors, N-Methyl-D-Aspartate metabolism Up-Regulation Guanine Nucleotide Exchange Factors physiology Long-Term Potentiation physiology Nerve Tissue Proteins physiology Synaptic Transmission physiology
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Language: English [Proc Natl Acad Sci U S A] 2016 Feb 23; Vol. 113 (8), pp. 2264-9. <i>Date of Electronic Publication: </i>2016 Feb 08. MeSH Terms: Guanine Nucleotide Exchange Factors / physiology ; Long-Term Potentiation / physiology ; Nerve Tissue Proteins / physiology ; Synaptic Transmission / physiology ; Animals ; CA1 Region, Hippocampal / physiology ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism ; Gene Knockdown Techniques ; Gene Knockout Techniques ; Guanine Nucleotide Exchange Factors / antagonists & inhibitors ; Guanine Nucleotide Exchange Factors / genetics ; HEK293 Cells ; Humans ; In Vitro Techniques ; Mice ; Models, Neurological ; Nerve Tissue Proteins / antagonists & inhibitors ; Nerve Tissue Proteins / genetics ; Phosphoproteins / antagonists & inhibitors ; Phosphoproteins / genetics ; Phosphoproteins / physiology ; Phosphorylation ; Protein Serine-Threonine Kinases / antagonists & inhibitors ; Protein Serine-Threonine Kinases / genetics ; Protein Serine-Threonine Kinases / physiology ; Rats ; Receptors, AMPA / metabolism ; Receptors, N-Methyl-D-Aspartate / metabolism ; Up-Regulation References: Neuron. 2005 Feb 17;45(4):525-38. (PMID: 15721239) ; Neuron. 2010 Nov 4;68(3):512-28. (PMID: 21040851) ; J Neurosci. 2005 Nov 16;25(46):10627-36. (PMID: 16291935) ; Mol Cell Neurosci. 2011 Jan;46(1):45-54. (PMID: 20708080) ; Nature. 2011 Apr 7;472(7341):100-4. (PMID: 21423166) ; J Proteome Res. 2011 Jun 3;10(6):2828-41. (PMID: 21488700) ; BMC Neurosci. 2011;12:126. (PMID: 22182308) ; Nat Rev Neurosci. 2012 Mar;13(3):169-82. (PMID: 22334212) ; Nature. 2013 Jan 24;493(7433):495-500. (PMID: 23235828) ; Mol Brain. 2013;6:5. (PMID: 23339575) ; Nat Neurosci. 2013 Aug;16(8):1154-61. (PMID: 23792946) ; Neuropharmacology. 2013 Nov;74:18-22. (PMID: 23439383) ; Neuron. 2013 Oct 30;80(3):704-17. (PMID: 24183021) ; Elife. 2014;3. doi: 10.7554/eLife.02839. (PMID: 25006034) ; Cold Spring Harb Perspect Biol. 2012 Jun;4(6). pii: a005710. doi: 10.1101/cshperspect.a005710. (PMID: 22510460) ; J Cell Sci. 2000 Feb;113 ( Pt 4):729-39. (PMID: 10652265) ; Cell. 2001 May 4;105(3):331-43. (PMID: 11348590) ; Nat Rev Neurosci. 2002 Mar;3(3):175-90. (PMID: 11994750) ; Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13902-7. (PMID: 12359873) ; Cell. 2003 Mar 7;112(5):631-43. (PMID: 12628184) ; J Neurosci Methods. 1991 Apr;37(2):173-82. (PMID: 1715499) ; J Neurophysiol. 1993 Oct;70(4):1451-9. (PMID: 7904300) ; J Biol Chem. 1999 Apr 30;274(18):12753-8. (PMID: 10212259) ; J Comp Neurol. 2005 Feb 21;482(4):333-48. (PMID: 15669055) ; Biol Cell. 2006 Mar;98(3):183-93. (PMID: 16033331) ; Neuron. 2006 Jul 20;51(2):213-25. (PMID: 16846856) ; Neuron. 2007 Nov 21;56(4):640-56. (PMID: 18031682) ; J Neurosci. 2008 Nov 19;28(47):12368-82. (PMID: 19020030) ; Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20953-8. (PMID: 19104036) ; Neuron. 2009 Apr 30;62(2):254-68. (PMID: 19409270) ; Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):13058-63. (PMID: 19625617) ; J Neurosci. 2010 Jun 30;30(26):8704-9. (PMID: 20592192) ; Gene. 2005 Feb 28;347(1):125-35. (PMID: 15715966) Grant Information: R00 MH103398 United States MH NIMH NIH HHS; R01 MH070957 United States MH NIMH NIH HHS Contributed Indexing: Keywords: CaMKII; Kalirin; LTP; Trio; spines Substance Nomenclature: 0 (Guanine Nucleotide Exchange Factors) ; 0 (KALRN protein, mouse) ; 0 (Kalrn protein, rat) ; 0 (Nerve Tissue Proteins) ; 0 (Phosphoproteins) ; 0 (Receptors, AMPA) ; 0 (Receptors, N-Methyl-D-Aspartate) ; 0 (Trio protein, mouse) ; 0 (Trio protein, rat) ; EC 2.7.11.1 (Protein Serine-Threonine Kinases) ; EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2) Entry Date(s): Date Created: 20160210 Date Completed: 20160725 Latest Revision: 20220113 Update Code: 20231215 PubMed Central ID: PMC4776457

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Kalirin and Trio proteins serve critical roles in excitatory synaptic transmission and LTP.