Sandbox Reserved 1654 - Revision history

Elsa Barbé at 15:21, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 15:21:03 GMT

←Older revision		Revision as of 15:21, 20 January 2022
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	=== ''' Function in memory ''' ===		=== ''' Function in memory ''' ===

		+	Long-term and short-term memories differ by the duration of their retention. Long-term memory formation needs transcription and translation of stored mRNAs. CPEB operate in the post synaptic domain of neurons. CPEB is stimulated by a neuronal stimulation, it “activates translation of CaMKII and similar mRNAs. It also associates with motor proteins for mRNA transport and has a role in packaging of bound mRNAs to RNP complexes. CPEB initiates polyadenylation induced translation of dormant mRNAs during Xenopus oocyte maturation. In developing oocytes, following nuclear export, CPE containing mRNAs are bound by CPEB1 as well as other interacting proteins like PARN (poly A ribonuclease) and Gld2 (polyA polymerase), leading to removal of polyA tail of mRNAs, as PARN overrides Gld2 activity. This leads to translational suppression of mRNAs. However upon activity-induced phosphorylation of CPEB, PARN dissociates from the complex and the mRNA is polyadenylated leading to translation.”
		+	[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5449092/]
	== ''' Diseases ''' ==		== ''' Diseases ''' ==
	CPEB proteins play a key role in some diseases, especially in cancers. Indeed, in some humans tumors the level of CPEB 1 is lower than in healthy cells and this leads to the growth of these tumors. An overexpression of CPEB 4 can lead to tumor growth too. Some researches try to find a cancer treatment thanks to CPEB mutations<ref name="publi" />.		CPEB proteins play a key role in some diseases, especially in cancers. Indeed, in some humans tumors the level of CPEB 1 is lower than in healthy cells and this leads to the growth of these tumors. An overexpression of CPEB 4 can lead to tumor growth too. Some researches try to find a cancer treatment thanks to CPEB mutations<ref name="publi" />.

Elsa Barbé at 14:39, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 14:39:43 GMT

←Older revision		Revision as of 14:39, 20 January 2022
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	== ''' Function ''' ==		== ''' Function ''' ==
		+	=== ''' General function ''' ===
	CPEB controls the balance between [https://en.wikipedia.org/wiki/Senescence senescence] and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.		CPEB controls the balance between [https://en.wikipedia.org/wiki/Senescence senescence] and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
	RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.		RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
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	On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase poly(A) polymerase] which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.		On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase poly(A) polymerase] which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.
		+
		+	=== ''' Function in memory ''' ===

	== ''' Diseases ''' ==		== ''' Diseases ''' ==

Elsa Barbé at 13:51, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:51:10 GMT

←Older revision		Revision as of 13:51, 20 January 2022
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	RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.		RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
	Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.		Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.
		+
		+	[[Image: CPEB-mediated translational control.jpg#filehistory\| thumb \|left\|360px\| upright=10/'''CPEB-mediated translational control''']]

	A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN] which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.		A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN] which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

Elsa Barbé at 13:24, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:24:16 GMT

←Older revision		Revision as of 13:24, 20 January 2022
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	***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.		***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
	** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref> [https://www.rcsb.org/structure/2MKK]		** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref> [https://www.rcsb.org/structure/2MKK]
-
	<table><tr><td colspan='3'><br>		<table><tr><td colspan='3'><br>
	</td></tr><tr id='Total Structure Weight'><td class="sblockLbl"><b>Total Structure Weight</b></td><td class="sblockDat"><span class='plainlinks'><scene name='86/868190/5czx_heavy_chain_labeled/1'>25,44kDa</scene></span></td></tr><tr id='Atom Count'><td class="sblockLbl"><b>Atom Count</b></td><td class="sblockDat"><span class='plainlinks'>1786</span></td></tr><tr id='Number of protein chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr> id='Number of nucleic acid chains'><td class="sblockLbl"><b>Number of nucleic acid chains</b></td><td class="sblockDat">1</td></tr>		</td></tr><tr id='Total Structure Weight'><td class="sblockLbl"><b>Total Structure Weight</b></td><td class="sblockDat"><span class='plainlinks'><scene name='86/868190/5czx_heavy_chain_labeled/1'>25,44kDa</scene></span></td></tr><tr id='Atom Count'><td class="sblockLbl"><b>Atom Count</b></td><td class="sblockDat"><span class='plainlinks'>1786</span></td></tr><tr id='Number of protein chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr> id='Number of nucleic acid chains'><td class="sblockLbl"><b>Number of nucleic acid chains</b></td><td class="sblockDat">1</td></tr>

Elsa Barbé at 13:23, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:23:21 GMT

←Older revision		Revision as of 13:23, 20 January 2022
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	<table><tr><td colspan='3'><br>		<table><tr><td colspan='3'><br>
-	</td></tr><tr id='Total Structure Weight'><td class="sblockLbl"><b>Total Structure Weight</b></td><td class="sblockDat"><span class='plainlinks'><scene name='86/868190/5czx_heavy_chain_labeled/1'>25,44kDa</scene></span></td></tr><tr id='Atom Count'><td class="sblockLbl"><b>Atom Count</b></td><td class="sblockDat"><span class='plainlinks'>1786</span></td></tr><tr id='Number of protein chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr> id='Number of nucleic acid chains'><td class="sblockLbl"><b>Number of ~~protein~~ chains</b></td><td class="sblockDat">1</td></tr>	+	</td></tr><tr id='Total Structure Weight'><td class="sblockLbl"><b>Total Structure Weight</b></td><td class="sblockDat"><span class='plainlinks'><scene name='86/868190/5czx_heavy_chain_labeled/1'>25,44kDa</scene></span></td></tr><tr id='Atom Count'><td class="sblockLbl"><b>Atom Count</b></td><td class="sblockDat"><span class='plainlinks'>1786</span></td></tr><tr id='Number of protein chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr> id='Number of nucleic acid chains'><td class="sblockLbl"><b>Number of nucleic acid chains</b></td><td class="sblockDat">1</td></tr>
		+

	<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>		<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>

Elsa Barbé at 13:22, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:22:51 GMT

←Older revision		Revision as of 13:22, 20 January 2022
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	***A 3<sub>10</sub> <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).		***A 3<sub>10</sub> <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
	***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.		***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
-	** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>	+	** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref> [https://www.rcsb.org/structure/2MKK]
		+
		+	<table><tr><td colspan='3'><br>
		+	</td></tr><tr id='Total Structure Weight'><td class="sblockLbl"><b>Total Structure Weight</b></td><td class="sblockDat"><span class='plainlinks'><scene name='86/868190/5czx_heavy_chain_labeled/1'>25,44kDa</scene></span></td></tr><tr id='Atom Count'><td class="sblockLbl"><b>Atom Count</b></td><td class="sblockDat"><span class='plainlinks'>1786</span></td></tr><tr id='Number of protein chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr> id='Number of nucleic acid chains'><td class="sblockLbl"><b>Number of protein chains</b></td><td class="sblockDat">1</td></tr>
		+
	<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>		<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>
	</StructureSection>		</StructureSection>

Elsa Barbé at 13:16, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:16:52 GMT

←Older revision		Revision as of 13:16, 20 January 2022
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	* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.		* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
	* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.		* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
-	** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>	+	** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref> [https://www.rcsb.org/structure/2M13]

	<table><tr><td colspan='3'><br>		<table><tr><td colspan='3'><br>

Elsa Barbé: Undo revision 3505541 by Elsa Barbé (Talk)

Elsa Barbé — Thu, 20 Jan 2022 13:12:28 GMT

Undo revision 3505541 by Elsa Barbé (Talk)

←Older revision		Revision as of 13:12, 20 January 2022
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	{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
	==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==		==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==
-	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] (which has a length of 65 amino acids) to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.	+	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1], which has a length of 65 amino acids, to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
	CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.		CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

Elsa Barbé at 13:12, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:12:13 GMT

←Older revision		Revision as of 13:12, 20 January 2022
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	{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
	==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==		==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==
-	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1], which has a length of 65 amino acids, to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.	+	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] (which has a length of 65 amino acids) to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
	CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.		CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

Elsa Barbé at 13:11, 20 January 2022

Elsa Barbé — Thu, 20 Jan 2022 13:11:41 GMT

←Older revision		Revision as of 13:11, 20 January 2022
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	{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
	==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==		==''' Cytoplasmic Polyadenylation Element-Binding Protein (CPEB) ''' ==
-	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.	+	[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1], which has a length of 65 amino acids, to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
	CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.		CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.