Group:MUZIC:ANKRD2 - Revision history

Jaime Prilusky at 11:32, 1 July 2015

Jaime Prilusky — Wed, 01 Jul 2015 11:32:13 GMT

←Older revision		Revision as of 11:32, 1 July 2015
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	== References ==		== References ==
	<references/>		<references/>
		+	[[Category: Z-disk]]

Nikos Pinotsis: /* Sequence Annotation */

Nikos Pinotsis — Tue, 02 Apr 2013 11:00:30 GMT

Sequence Annotation

←Older revision		Revision as of 11:00, 2 April 2013
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	== Sequence Annotation ==		== Sequence Annotation ==
	Ankrd2 is comprising 360 amino acids and all sequences are available in Uniprot:		Ankrd2 is comprising 360 amino acids and all sequences are available in Uniprot:
-	[~~http://~~http://www.uniprot.org/uniprot/Q9GZV1 human], [http://www.uniprot.org/uniprot/Q9WV06 mouse], [http://www.uniprot.org/uniprot/F1MX12 bovine].	+	[http://www.uniprot.org/uniprot/Q9GZV1 human], [http://www.uniprot.org/uniprot/Q9WV06 mouse], [http://www.uniprot.org/uniprot/F1MX12 bovine].
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Nikos Pinotsis: /* Sequence Annotation */

Nikos Pinotsis — Tue, 02 Apr 2013 10:55:43 GMT

Sequence Annotation

←Older revision		Revision as of 10:55, 2 April 2013
Line 7:		Line 7:
	== Sequence Annotation ==		== Sequence Annotation ==
	Ankrd2 is comprising 360 amino acids and all sequences are available in Uniprot:		Ankrd2 is comprising 360 amino acids and all sequences are available in Uniprot:
-	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine].	+	[http://http://www.uniprot.org/uniprot/Q9GZV1 human], [http://www.uniprot.org/uniprot/Q9WV06 mouse], [http://www.uniprot.org/uniprot/F1MX12 bovine].
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Nikos Pinotsis at 12:41, 11 February 2013

Nikos Pinotsis — Mon, 11 Feb 2013 12:41:43 GMT

←Older revision		Revision as of 12:41, 11 February 2013
Line 6:		Line 6:

	== Sequence Annotation ==		== Sequence Annotation ==
-	Ankrd2 is comprising 360 amino acids and ~~the sequence~~	+	Ankrd2 is comprising 360 amino acids and all sequences are available in Uniprot:
-	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine]~~, Ankrd2 is available from Uniprot~~.	+	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine].
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Nikos Pinotsis at 12:39, 11 February 2013

Nikos Pinotsis — Mon, 11 Feb 2013 12:39:53 GMT

←Older revision		Revision as of 12:39, 11 February 2013
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-	== '''ANKRD2''' ==	+	=== '''ANKRD2''' ===

-	~~'''~~Introduction~~'''~~	+	==Introduction==

	Ankyrin repeat-containing protein 2 (stretch responsive muscle) '''Ankrd2''' belongs to the conserved muscle ankyrin repeat protein (MARP) family<ref name='one'>PMID 10873377</ref> also known as ARPP<ref name='two'>PMID 11453652</ref>. It is mainly expressed in then skeletal muscle and less in the cardiac muscle, preferentially in type 1 fibers<ref name='three'>PMID 12004005</ref>. Ankrd2 shares approximately 50% sequence homology with two more MARP family members: the cardiac ankyrin repeat protein (CARP/Ankrd1) and the diabetes related ankyrin repeat protein DARP. Expression of Ankrd2/Arpp is induced in response to various forms of stress and is highly responsive to muscle mechanical status both in vivo and in vitro<ref name='one'>PMID 10873377</ref>,<ref name='four'>PMID 14583192</ref>, as well as to muscle plasticity induced by physical exercise<ref name='five'>PMID 14561590</ref>,<ref name='six'>PMID 15677738</ref>. Apart from the mechanosensory function, Ankrd2/Arpp is a negative regulator of muscle differentiation<ref name='seven'>PMID 18302940</ref>.		Ankyrin repeat-containing protein 2 (stretch responsive muscle) '''Ankrd2''' belongs to the conserved muscle ankyrin repeat protein (MARP) family<ref name='one'>PMID 10873377</ref> also known as ARPP<ref name='two'>PMID 11453652</ref>. It is mainly expressed in then skeletal muscle and less in the cardiac muscle, preferentially in type 1 fibers<ref name='three'>PMID 12004005</ref>. Ankrd2 shares approximately 50% sequence homology with two more MARP family members: the cardiac ankyrin repeat protein (CARP/Ankrd1) and the diabetes related ankyrin repeat protein DARP. Expression of Ankrd2/Arpp is induced in response to various forms of stress and is highly responsive to muscle mechanical status both in vivo and in vitro<ref name='one'>PMID 10873377</ref>,<ref name='four'>PMID 14583192</ref>, as well as to muscle plasticity induced by physical exercise<ref name='five'>PMID 14561590</ref>,<ref name='six'>PMID 15677738</ref>. Apart from the mechanosensory function, Ankrd2/Arpp is a negative regulator of muscle differentiation<ref name='seven'>PMID 18302940</ref>.

Nikos Pinotsis at 20:19, 20 January 2013

Nikos Pinotsis — Sun, 20 Jan 2013 20:19:58 GMT

←Older revision		Revision as of 20:19, 20 January 2013
Line 8:		Line 8:
	Ankrd2 is comprising 360 amino acids and the sequence		Ankrd2 is comprising 360 amino acids and the sequence
	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], Ankrd2 is available from Uniprot.		[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], Ankrd2 is available from Uniprot.
-	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />	+	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs (PDB entry: [http://www.pdb.org/pdb/explore/explore.do?structureId=2qyj 2qyj])' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

	== Structure ==		== Structure ==

-	~~Ankrd2~~ gene contains 9 exons and spans about 12 kb. The 280 bp long region upstream of the transcription initiation site of the human Ankrd2 gene is sufficient to confer spatial and temporal expression specificity, and contains mainly cis-elements specific for the muscle-specific transcription factor MyoD and for NF-kB. <ref name='eight'>PMID 11444853</ref> ~~Ankrd2~~ promoter activity is significantly up-regulated by Nkx2.5 <ref name='nine'>PMID 22016770</ref>, upon longitudinal stretch by Akt-dependent NF-kB signaling pathway and in response to transverse stretch by Raf-1-dependent AP-1 signaling pathway. <ref name='ten'>PMID 20442316</ref> The major structural characteristic of the Ankrd2 protein is the presence in the middle portion of four conserved copies of 33-residue ankyrin repeats. In addition Ankrd2 contains a coiled-coil domain that contributes to its self-dimerization, a nuclear localization signal (NLS), allowing its sorting to the nucleus, PEST protein degradation sequence and numerous potential modification sites, mainly for phosphorylation. In particular the phosphorylation of Ankrd2 by the serine/threonine kinase ~~Akt 2~~ is important for its function in muscle differentiation. <ref name='eleven'>PMID 21737686</ref> The position of Ankrd2 phosphorylation by ~~Akt 2~~ is ~~Ser 72~~ which is in close proximity of ~~calpain 3~~ cleavage site (Arg 77). There are many other consensus phosphorylation sites for casein kinase I (CKI), casein kinase II (CKII), protein kinase C (PKC), extracellular signal regulated kinase (ERK), cAMP- dependent protein kinase, calmodulin-dependent protein kinase II and cGMP-dependent protein kinase <ref name='two'>PMID 11453652</ref>,<ref name='four'>PMID 14583192</ref>	+	The ankrd2 gene contains 9 exons and spans about 12 kb. The 280 bp long region upstream of the transcription initiation site of the human Ankrd2 gene is sufficient to confer spatial and temporal expression specificity and contains mainly cis-elements specific for the muscle-specific transcription factor MyoD and for NF-kB<ref name='eight'>PMID 11444853</ref>. The ankrd2 promoter activity is significantly up-regulated by Nkx2.5<ref name='nine'>PMID 22016770</ref> upon longitudinal stretch by Akt-dependent NF-kB signaling pathway and in response to transverse stretch by Raf-1-dependent AP-1 signaling pathway<ref name='ten'>PMID 20442316</ref>. The major structural characteristic of the Ankrd2 protein is the presence in the middle portion of four conserved copies of the 33-residue ankyrin repeats. In addition, Ankrd2 contains a coiled-coil domain that contributes to its self-dimerization, a nuclear localization signal (NLS) allowing its sorting to the nucleus, a PEST protein degradation sequence and numerous potential modification sites mainly for phosphorylation. In particular the phosphorylation of Ankrd2 by the serine/threonine kinase Akt2 is important for its function in muscle differentiation<ref name='eleven'>PMID 21737686</ref>. The position of Ankrd2 phosphorylation by Akt2 is Ser72 which is in close proximity of a calpain3 cleavage site (Arg 77). There are many other consensus phosphorylation sites for casein kinase I (CKI), casein kinase II (CKII), protein kinase C (PKC), extracellular signal regulated kinase (ERK), cAMP- dependent protein kinase, calmodulin-dependent protein kinase II and cGMP-dependent protein kinase <ref name='two'>PMID 11453652</ref>,<ref name='four'>PMID 14583192</ref>.


Line 20:		Line 20:
	== Gene Function and Interactions ==		== Gene Function and Interactions ==

-	Ankrd2 is involved in muscle stress response. It is up-regulated after chronic immobilization in a stretched position.<ref name='one'>PMID 10873377</ref> <ref name='six'>PMID 15677738</ref>, after eccentric contraction <ref name='five'>PMID 14561590</ref> , as well as in injured muscles.<ref name='eleven'>PMID 17926058</ref> Denervation of slow muscle decreases the level of Ankrd2 to below the detection limit in 4 weeks <ref name='six'>PMID 15677738</ref>, whereas denervation of fast muscle increases its expression.<ref name='three'>PMID 12004005</ref>	+	Ankrd2 is involved in muscle stress response. It is up-regulated after chronic immobilization in a stretched position<ref name='one'>PMID 10873377</ref>,<ref name='six'>PMID 15677738</ref>, after eccentric contraction<ref name='five'>PMID 14561590</ref>, as well as in injured muscles<ref name='eleven'>PMID 17926058</ref>. Denervation of slow muscle decreases the level of Ankrd2 to below the detection limit in 4 weeks <ref name='six'>PMID 15677738</ref>, whereas denervation of fast muscle increases its expression.<ref name='three'>PMID 12004005</ref>
-	Ankrd2 is found in the central I-band of the sarcomere, where binds the N2A region of titin. In myoblasts Ankrd2 localizes both in the nuclei, in form of speckles and in the cytoplasm <ref name='seven'>PMID 18302940</ref>, with a diffused pattern. As the differentiation into multinucleated myotubes progresses, Ankrd2 seems to change localization and to accumulate mainly in the cytoplasm <ref>pmid 11444853 </ref>. In general, Ankrd2 protein functions by ~~moving~~ between the sarcomere and the nucleus, mainly in response to stress signals <ref name='fourteen'>PMID 15136035 </ref>.	+	Ankrd2 is found in the central I-band of the sarcomere, where binds the N2A region of titin. In myoblasts Ankrd2 localizes both in the nuclei, in form of speckles and in the cytoplasm<ref name='seven'>PMID 18302940</ref>, with a diffused pattern. As the differentiation into multinucleated myotubes progresses, Ankrd2 seems to change localization and to accumulate mainly in the cytoplasm<ref>pmid 11444853 </ref>. In general, Ankrd2 protein functions by suffling between the sarcomere and the nucleus, mainly in response to stress signals<ref name='fourteen'>PMID 15136035 </ref>.
-	Ankrd2 is not essential for the basal functioning of skeletal muscle, but it is clear its influence on the gene expression program of skeletal muscle cells.<ref name='thirteen'>PMID 17392382</ref> Mainly the Ankrd2 protein has a major role in skeletal muscle formation as a myogenic regulator, since its over-expression in C2C12 myoblasts significantly affects and down-regulates MyoD, myogenin, and their target gene Myh1.<ref name='seven'>PMID 18302940</ref>	+	Ankrd2 is not essential for the basal functioning of skeletal muscle, but it is clear its influence on the gene expression program of skeletal muscle cells<ref name='thirteen'>PMID 17392382</ref>. Mainly the Ankrd2 protein has a major role in skeletal muscle formation as a myogenic regulator since its over-expression in C2C12 myoblasts significantly affects and down-regulates MyoD, myogenin and their target gene Myh1<ref name='seven'>PMID 18302940</ref>.


	==Pathology ==		==Pathology ==
-	Altered expression of Ankrd2 has been found in patients suffering from inherited myopathies (muscular dystrophies (MD), congenital myopathies (CM)) and motor neuron diseases (spinal muscular atrophy (SMA), amyotrophic lateral sclerosis (ALS)).The Ankrd2/Arpp can interact with titin <ref name='four'>PMID 14583192</ref>, telethonin/T-cap <ref name='fourteen'>PMID 15136035 </ref>, calpain 3 <ref name='fifteen'>PMID 18310072 </ref>, promyelocytic leukemia protein (PML)<ref name='fourteen'>PMID 15136035 </ref>, YB-1 <ref name='fourteen'>PMID 15136035 </ref>, p53 <ref name='fourteen'>PMID 15136035 </ref>, ~~Akt 2~~ <ref name='eleven'>PMID 21737686</ref> and zonula occludens 1 (ZO1).<ref name='nine'>PMID 22016770</ref>	+	Altered expression of Ankrd2 has been found in patients suffering from inherited myopathies (muscular dystrophies (MD), congenital myopathies (CM)) and motor neuron diseases (spinal muscular atrophy (SMA), amyotrophic lateral sclerosis (ALS)).The Ankrd2/Arpp can interact with titin<ref name='four'>PMID 14583192</ref>, telethonin/T-cap<ref name='fourteen'>PMID 15136035 </ref>, calpain 3<ref name='fifteen'>PMID 18310072 </ref>, promyelocytic leukemia protein (PML)<ref name='fourteen'>PMID 15136035 </ref>, YB-1<ref name='fourteen'>PMID 15136035 </ref>, p53<ref name='fourteen'>PMID 15136035 </ref>, Akt2<ref name='eleven'>PMID 21737686</ref> and zonula occludens 1 (ZO1)<ref name='nine'>PMID 22016770</ref>.

Nikos Pinotsis at 20:12, 20 January 2013

Nikos Pinotsis — Sun, 20 Jan 2013 20:12:19 GMT

←Older revision		Revision as of 20:12, 20 January 2013
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	'''Introduction'''		'''Introduction'''

-	Ankyrin repeat-containing protein 2 (stretch responsive muscle) '''Ankrd2''' belongs to the conserved muscle ankyrin repeat protein (MARP) family,<ref name='one'>PMID 10873377</ref> ~~Also~~ known as ~~Arpp.~~<ref name='two'>PMID 11453652</ref> It is ~~more~~ expressed in skeletal ~~than~~ cardiac muscle, preferentially in type 1 fibers.<ref name='three'>PMID 12004005</ref> Ankrd2 shares approximately 50% homology with ~~the~~ two more MARP family members: ~~Cardiac~~ ankyrin repeat protein (CARP/Ankrd1) and ~~Diabetes~~ related ankyrin repeat protein DARP.Expression of Ankrd2/Arpp is induced in response to various forms of stress and is highly responsive to muscle mechanical status both in vivo and in vitro <ref name='one'>PMID 10873377</ref>,<ref name='four'>PMID 14583192</ref>, as well as to muscle plasticity induced by physical exercise <ref name='five'>PMID 14561590</ref>,<ref name='six'>PMID 15677738</ref>. Apart from the mechanosensory function, Ankrd2/Arpp is a negative regulator of muscle differentiation.<ref name='seven'>PMID 18302940</ref>	+	Ankyrin repeat-containing protein 2 (stretch responsive muscle) '''Ankrd2''' belongs to the conserved muscle ankyrin repeat protein (MARP) family<ref name='one'>PMID 10873377</ref> also known as ARPP<ref name='two'>PMID 11453652</ref>. It is mainly expressed in then skeletal muscle and less in the cardiac muscle, preferentially in type 1 fibers<ref name='three'>PMID 12004005</ref>. Ankrd2 shares approximately 50% sequence homology with two more MARP family members: the cardiac ankyrin repeat protein (CARP/Ankrd1) and the diabetes related ankyrin repeat protein DARP. Expression of Ankrd2/Arpp is induced in response to various forms of stress and is highly responsive to muscle mechanical status both in vivo and in vitro<ref name='one'>PMID 10873377</ref>,<ref name='four'>PMID 14583192</ref>, as well as to muscle plasticity induced by physical exercise<ref name='five'>PMID 14561590</ref>,<ref name='six'>PMID 15677738</ref>. Apart from the mechanosensory function, Ankrd2/Arpp is a negative regulator of muscle differentiation<ref name='seven'>PMID 18302940</ref>.

	== Sequence Annotation ==		== Sequence Annotation ==
-	Ankrd2 is ~~comprised of~~ 360 amino acids, the sequence of	+	Ankrd2 is comprising 360 amino acids and the sequence
	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], Ankrd2 is available from Uniprot.		[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], Ankrd2 is available from Uniprot.
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Narendra Kumar Verma at 10:45, 16 November 2012

Narendra Kumar Verma — Fri, 16 Nov 2012 10:45:28 GMT

←Older revision		Revision as of 10:45, 16 November 2012
Line 7:		Line 7:
	== Sequence Annotation ==		== Sequence Annotation ==
	Ankrd2 is comprised of 360 amino acids, the sequence of		Ankrd2 is comprised of 360 amino acids, the sequence of
-	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], ~~[http://www.uniprot.org/uniprot/A4GR69 porcine]~~ Ankrd2 is available from Uniprot.	+	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], Ankrd2 is available from Uniprot.
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Narendra Kumar Verma at 10:44, 16 November 2012

Narendra Kumar Verma — Fri, 16 Nov 2012 10:44:47 GMT

←Older revision		Revision as of 10:44, 16 November 2012
Line 6:		Line 6:

	== Sequence Annotation ==		== Sequence Annotation ==
-	http://www.uniprot.org/uniprot/Q9GZV1	+	Ankrd2 is comprised of 360 amino acids, the sequence of
		+	[http://http://www.uniprot.org/uniprot/ Q9GZV1 human], [http://www.uniprot.org/uniprot/ Q9WV06 mouse], [http://www.uniprot.org/uniprot/ F1MX12 bovine], [http://www.uniprot.org/uniprot/A4GR69 porcine] Ankrd2 is available from Uniprot.
	<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />		<Structure load='2QYJ' size='300' frame='true' align='right' caption='Structure of a designed ankyrin repeat protein (DARPin) with five ankyrin repeat motifs [[2qyj]]' scene='User:Spyros_D._Chatziefthimiou/workbench/ANKRD2/2qyj/1' />

Narendra Kumar Verma at 09:40, 16 November 2012

Narendra Kumar Verma — Fri, 16 Nov 2012 09:40:37 GMT

←Older revision		Revision as of 09:40, 16 November 2012
Line 20:		Line 20:

	Ankrd2 is involved in muscle stress response. It is up-regulated after chronic immobilization in a stretched position.<ref name='one'>PMID 10873377</ref> <ref name='six'>PMID 15677738</ref>, after eccentric contraction <ref name='five'>PMID 14561590</ref> , as well as in injured muscles.<ref name='eleven'>PMID 17926058</ref> Denervation of slow muscle decreases the level of Ankrd2 to below the detection limit in 4 weeks <ref name='six'>PMID 15677738</ref>, whereas denervation of fast muscle increases its expression.<ref name='three'>PMID 12004005</ref>		Ankrd2 is involved in muscle stress response. It is up-regulated after chronic immobilization in a stretched position.<ref name='one'>PMID 10873377</ref> <ref name='six'>PMID 15677738</ref>, after eccentric contraction <ref name='five'>PMID 14561590</ref> , as well as in injured muscles.<ref name='eleven'>PMID 17926058</ref> Denervation of slow muscle decreases the level of Ankrd2 to below the detection limit in 4 weeks <ref name='six'>PMID 15677738</ref>, whereas denervation of fast muscle increases its expression.<ref name='three'>PMID 12004005</ref>
		+	Ankrd2 is found in the central I-band of the sarcomere, where binds the N2A region of titin. In myoblasts Ankrd2 localizes both in the nuclei, in form of speckles and in the cytoplasm <ref name='seven'>PMID 18302940</ref>, with a diffused pattern. As the differentiation into multinucleated myotubes progresses, Ankrd2 seems to change localization and to accumulate mainly in the cytoplasm <ref>pmid 11444853 </ref>. In general, Ankrd2 protein functions by moving between the sarcomere and the nucleus, mainly in response to stress signals <ref name='fourteen'>PMID 15136035 </ref>.
	Ankrd2 is not essential for the basal functioning of skeletal muscle, but it is clear its influence on the gene expression program of skeletal muscle cells.<ref name='thirteen'>PMID 17392382</ref> Mainly the Ankrd2 protein has a major role in skeletal muscle formation as a myogenic regulator, since its over-expression in C2C12 myoblasts significantly affects and down-regulates MyoD, myogenin, and their target gene Myh1.<ref name='seven'>PMID 18302940</ref>		Ankrd2 is not essential for the basal functioning of skeletal muscle, but it is clear its influence on the gene expression program of skeletal muscle cells.<ref name='thirteen'>PMID 17392382</ref> Mainly the Ankrd2 protein has a major role in skeletal muscle formation as a myogenic regulator, since its over-expression in C2C12 myoblasts significantly affects and down-regulates MyoD, myogenin, and their target gene Myh1.<ref name='seven'>PMID 18302940</ref>

-
-	==Localization==
-	Ankrd2 is found in the central I-band of the sarcomere, where binds the N2A region of titin. In myoblasts Ankrd2 localizes both in the nuclei, in form of speckles and in the cytoplasm <ref name='seven'>PMID 18302940</ref>, with a diffused pattern. As the differentiation into multinucleated myotubes progresses, Ankrd2 seems to change localization and to accumulate mainly in the cytoplasm <ref>pmid 11444853 </ref>. In general, Ankrd2 protein functions by moving between the sarcomere and the nucleus, mainly in response to stress signals <ref name='fourteen'>PMID 15136035 </ref>.

	==Pathology ==		==Pathology ==