LTP Pathway - Revision history

Monakhos: Changing image note:
Changing image note: <div align="center" style="position: absolute; left: 0px; right: 0px; top: 0px; bottom: 0px;> CaMKII</div>CaMKII -- Ca2+/calmodu

← Older revision Revision as of 01:59, 15 April 2013
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CaMKII

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[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.
[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.

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Monakhos: Adding image note: Cyclic AMP or cAMP works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetra

2013-04-15T07:48:00Z

Adding image note: Cyclic AMP or cAMP works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetra

← Older revision		Revision as of 00:48, 15 April 2013
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	[[Arc]], for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 1995. Arc is a member of the immediate-early gene (IEG) family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors. Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning and memory-related molecular processes. Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization, and utility as a marker for plastic changes in the brain. Along with other IEGs such as zif268 and Homer 1a, Arc is also a significant tool for systems neuroscience as illustrated by the development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).		[[Arc]], for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 1995. Arc is a member of the immediate-early gene (IEG) family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors. Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning and memory-related molecular processes. Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization, and utility as a marker for plastic changes in the brain. Along with other IEGs such as zif268 and Homer 1a, Arc is also a significant tool for systems neuroscience as illustrated by the development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).
	{{ImageNoteEnd\|id=6}}		{{ImageNoteEnd\|id=6}}
			{{ImageNote\|id=7\|x=372\|y=729\|w=55\|h=32\|dimx=1584\|dimy=1584\|style=2}}
			[[Cyclic AMP]] or [[cAMP]] works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetrameric holoenzyme, consisting of two catalytic and two regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins.
			There are some minor PKA-independent functions of cAMP, e.g., activation of calcium channels, providing a minor pathway by which growth hormone-releasing hormone causes a release of growth hormone.
			{{ImageNoteEnd\|id=7}}
	</div>		</div>
	</div>		</div>

Monakhos: Adding image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 19

2013-04-15T07:47:38Z

Adding image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 19

← Older revision		Revision as of 00:47, 15 April 2013
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	4. PKA can directly activate CREB, which binds CRE, altering the transcription		4. PKA can directly activate CREB, which binds CRE, altering the transcription
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			{{ImageNote\|id=6\|x=942\|y=390\|w=61\|h=42\|dimx=1584\|dimy=1584\|style=2}}
			[[Arc]], for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 1995. Arc is a member of the immediate-early gene (IEG) family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors. Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning and memory-related molecular processes. Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization, and utility as a marker for plastic changes in the brain. Along with other IEGs such as zif268 and Homer 1a, Arc is also a significant tool for systems neuroscience as illustrated by the development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).
			{{ImageNoteEnd\|id=6}}
	</div>		</div>
	</div>		</div>

Monakhos: Changing image note: PKA or Protein Kinase A 1. concentration of cAMP rises (e.g., activation of adenylate cyclase via GPCR-Gs) 2. cAMP molecules

2013-04-15T07:47:16Z

Changing image note: PKA or Protein Kinase A 1. concentration of cAMP rises (e.g., activation of adenylate cyclase via GPCR-Gs) 2. cAMP molecules

← Older revision		Revision as of 00:47, 15 April 2013
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	{{ImageNote\|id=5\|x=414\|y=655\|w=57\|h=36\|dimx=1584\|dimy=1584\|style=2}}		{{ImageNote\|id=5\|x=414\|y=655\|w=57\|h=36\|dimx=1584\|dimy=1584\|style=2}}
	[[~~Arc~~]]~~, for activity-regulated cytoskeleton-associated protein~~ (~~also known as Arg3~~.1), ~~is a plasticity protein first characterized in 1995. Arc is a member~~ of ~~the immediate~~-~~early gene (IEG~~) ~~family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors~~. ~~Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning~~ and ~~memory-related molecular processes~~. ~~Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization,~~ and ~~utility as a marker for plastic changes in the brain~~. ~~Along with other IEGs such as zif268 and Homer 1a~~, ~~Arc is also a significant tool for systems neuroscience as illustrated by~~ the ~~development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).~~		[[PKA]] or [[Protein Kinase A]]

			1. concentration of cAMP rises (e.g., activation of adenylate cyclase via GPCR-Gs)

			2. cAMP molecules bind and release each PKA regulatory subunit.

			3. catalytic subunits phosphorylate Ser and Thr residues

			4. PKA can directly activate CREB, which binds CRE, altering the transcription
	{{ImageNoteEnd\|id=5}}		{{ImageNoteEnd\|id=5}}
	</div>		</div>

Monakhos: Removing image note: Cyclic AMP or cAMP works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tet

2013-04-15T07:46:17Z

Removing image note: Cyclic AMP or cAMP works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tet

← Older revision		Revision as of 00:46, 15 April 2013
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	<div class="wpImageAnnotatorFile">[[File:LTP Pathway1.png\|800px]]</div>		<div class="wpImageAnnotatorFile">[[File:LTP Pathway1.png\|800px]]</div>
	<div style="display:none;"><div><div><!--Dummy marker to have image notes inserted below this line-->{{ImageNoteEnd\|id=-1}}		<div style="display:none;"><div><div><!--Dummy marker to have image notes inserted below this line-->{{ImageNoteEnd\|id=-1}}
	~~{{ImageNote\|id=2\|x=638\|y=537\|w=61\|h=30\|dimx=1584\|dimy=1584\|style=2}}~~
	[[Cyclic AMP]] or [[cAMP]] works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetrameric holoenzyme, consisting of two catalytic and two regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins.
	~~There are some minor PKA-independent functions of cAMP, e.g., activation of calcium channels, providing a minor pathway by which growth hormone-releasing hormone causes a release of growth hormone.~~
	~~{{ImageNoteEnd\|id=2}}~~
	{{ImageNote\|id=4\|x=406\|y=612\|w=71\|h=38\|dimx=1584\|dimy=1584\|style=2}}		{{ImageNote\|id=4\|x=406\|y=612\|w=71\|h=38\|dimx=1584\|dimy=1584\|style=2}}
	[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.		[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.

Monakhos: Removing image note: PKA or Protein Kinase A 1. concentration of cAMP rises (e.g., activation of adenylate cyclase via GPCR-Gs) 2. cAMP molecules

2013-04-15T07:45:57Z

Removing image note: PKA or Protein Kinase A 1. concentration of cAMP rises (e.g., activation of adenylate cyclase via GPCR-Gs) 2. cAMP molecules

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 There are some minor PKA-independent functions of cAMP, e.g., activation of calcium channels, providing a minor pathway by which growth hormone-releasing hormone causes a release of growth hormone.
 {{ImageNoteEnd|id=2}}
 {{ImageNote|id=4|x=406|y=612|w=71|h=38|dimx=1584|dimy=1584|style=2}}
 [[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.

Monakhos: Adding image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 19

2013-04-15T07:45:32Z

Adding image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 19

← Older revision		Revision as of 00:45, 15 April 2013
Line 149:		Line 149:
	[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.		[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.
	{{ImageNoteEnd\|id=4}}		{{ImageNoteEnd\|id=4}}
			{{ImageNote\|id=5\|x=414\|y=655\|w=57\|h=36\|dimx=1584\|dimy=1584\|style=2}}
			[[Arc]], for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 1995. Arc is a member of the immediate-early gene (IEG) family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors. Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning and memory-related molecular processes. Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization, and utility as a marker for plastic changes in the brain. Along with other IEGs such as zif268 and Homer 1a, Arc is also a significant tool for systems neuroscience as illustrated by the development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).
			{{ImageNoteEnd\|id=5}}
	</div>		</div>
	</div>		</div>

Monakhos: Adding image note: CaMKII -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmod

2013-04-15T07:45:03Z

Adding image note: CaMKII -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmod

← Older revision		Revision as of 00:45, 15 April 2013
Line 146:		Line 146:
	4. PKA can directly activate CREB, which binds CRE, altering the transcription		4. PKA can directly activate CREB, which binds CRE, altering the transcription
	{{ImageNoteEnd\|id=3}}		{{ImageNoteEnd\|id=3}}
			{{ImageNote\|id=4\|x=406\|y=612\|w=71\|h=38\|dimx=1584\|dimy=1584\|style=2}}
			[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.
			{{ImageNoteEnd\|id=4}}
	</div>		</div>
	</div>		</div>

Monakhos: Removing image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in

2013-04-15T07:44:37Z

Removing image note: Arc, for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in

← Older revision		Revision as of 00:44, 15 April 2013
Line 131:		Line 131:
	<div class="wpImageAnnotatorFile">[[File:LTP Pathway1.png\|800px]]</div>		<div class="wpImageAnnotatorFile">[[File:LTP Pathway1.png\|800px]]</div>
	<div style="display:none;"><div><div><!--Dummy marker to have image notes inserted below this line-->{{ImageNoteEnd\|id=-1}}		<div style="display:none;"><div><div><!--Dummy marker to have image notes inserted below this line-->{{ImageNoteEnd\|id=-1}}
	~~{{ImageNote\|id=1\|x=392\|y=640\|w=46\|h=28\|dimx=1584\|dimy=1584\|style=2}}~~
	[[Arc]], for activity-regulated cytoskeleton-associated protein (also known as Arg3.1), is a plasticity protein first characterized in 1995. Arc is a member of the immediate-early gene (IEG) family, a rapidly activated class of genes functionally defined by their ability to be transcribed in the presence of protein synthesis inhibitors. Arc mRNA is localized to activated synaptic sites in an NMDA receptor-dependent manner, where the newly translated protein is believed to play a critical role in learning and memory-related molecular processes. Arc is widely considered to be an important protein in neurobiology because of its activity regulation, localization, and utility as a marker for plastic changes in the brain. Along with other IEGs such as zif268 and Homer 1a, Arc is also a significant tool for systems neuroscience as illustrated by the development of the cellular compartment analysis of temporal activity by fluorescence in situ hybridization, or catFISH technique (see fluorescent in situ hybridization).
	~~{{ImageNoteEnd\|id=1}}~~
	{{ImageNote\|id=2\|x=638\|y=537\|w=61\|h=30\|dimx=1584\|dimy=1584\|style=2}}		{{ImageNote\|id=2\|x=638\|y=537\|w=61\|h=30\|dimx=1584\|dimy=1584\|style=2}}
	[[Cyclic AMP]] or [[cAMP]] works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetrameric holoenzyme, consisting of two catalytic and two regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins.		[[Cyclic AMP]] or [[cAMP]] works by activating protein kinase A (PKA, cAMP-dependent protein kinase). PKA is normally inactive as a tetrameric holoenzyme, consisting of two catalytic and two regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins.

Monakhos: Removing image note: CaMKII -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calm

2013-04-15T07:43:57Z

Removing image note: CaMKII -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calm

← Older revision		Revision as of 00:43, 15 April 2013
Line 149:		Line 149:
	4. PKA can directly activate CREB, which binds CRE, altering the transcription		4. PKA can directly activate CREB, which binds CRE, altering the transcription
	{{ImageNoteEnd\|id=3}}		{{ImageNoteEnd\|id=3}}
	~~{{ImageNote\|id=4\|x=398\|y=586\|w=75\|h=38\|dimx=1584\|dimy=1584\|style=2}}~~
	[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.

	~~CaMKII has also been shown to aid in the process of AMPA receptor exocytosis. CaMKII activity leads to endosomal docking at the membrane.~~
	~~{{ImageNoteEnd\|id=4}}~~
	</div>		</div>
	</div>		</div>

← Older revision		Revision as of 01:59, 15 April 2013
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			<div align="center" style="position: absolute; left: 0px; right: 0px; top: 0px; bottom: 0px;>
			CaMKII
			</div>

	[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.		[[CaMKII]] -- Ca2+/calmodulin-dependent protein kinases II are serine/threonine-specific protein kinases that are regulated by the calmodulin complex. CaMKII phosphorylates AMPA receptors at the P2 serine 831 site. This increases channel conductance of GluA1 subunits of AMPA receptors.
	{{ImageNoteEnd\|id=4}}		{{ImageNoteEnd\|id=4}}