ANKRD2

Last updated
ANKRD2
Identifiers
Aliases ANKRD2 , ankyrin repeat domain 2 (stretch responsive muscle), ARPP, ankyrin repeat domain 2
External IDs OMIM: 610734 MGI: 1861447 HomoloGene: 10568 GeneCards: ANKRD2
Orthologs
SpeciesHumanMouse
Entrez

26287

56642

Ensembl

ENSG00000165887

ENSMUSG00000025172

UniProt

Q9GZV1

Q9WV06

RefSeq (mRNA)

NM_020349
NM_001129981
NM_001291218
NM_001291219
NM_001346793

Contents

NM_020033

RefSeq (protein)

NP_001123453
NP_001278147
NP_001278148
NP_001333722
NP_065082

NP_064417

Location (UCSC) Chr 10: 97.57 – 97.58 Mb Chr 19: 42.02 – 42.03 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ankyrin Repeat, PEST sequence and Proline-rich region (ARPP), also known as Ankyrin repeat domain-containing protein 2 is a protein that in humans is encoded by the ANKRD2 gene. [5] [6] [7] [8] ARPP is a member of the muscle ankyrin repeat proteins (MARP), which also includes CARP and DARP, and is highly expressed in cardiac and skeletal muscle and in other tissues. Expression of ARPP has been shown to be altered in patients with dilated cardiomyopathy and amyotrophic lateral sclerosis. A role for Ankrd2 in tumor progression and metastases spreading has also been described. [9] [10]

Structure

Two isoforms of ARPP have been documented; a 39.8 kDa protein isoform composed of 360 amino acids [11] and a 36.2 kDa protein isoform composed of 327 amino acids. [12] ANKRD2 has nine exons, four of which encode ankyrin repeats in the middle region of the protein, a PEST-like and Lysine-rich sequence in the N-terminal region, and a Proline-rich sequence containing consensus sequences for phosphorylation in the C-terminal region. [13] [14] It has been proposed that ARPP can homo- or hetero-dimerize with other MARPs in an antiparallel fashion. [15] ARPP is highly expressed in nuclei and I-bands in slow skeletal fibers [13] [16] and cardiac muscle, specifically in ventricular regions [14] at intercalated discs; [17] and expression in brain, pancreas and esophageal epithelium has also been documented. [16] [18] Though ARPP and CARP proteins show significant homology, their expression profiles in muscle cells are markedly different; CARP is expressed throughout atria and ventricles, in development and in adult myocytes, however ARPP is almost exclusively ventricular and only in adult myocytes. ARPP was also found to be expressed in rhabdomyosarcomas, exhibiting a pattern distinct from actin and desmin. [19]

Function

ARPP localizes to both nuclei and sarcomeres in muscle cells. ARPP may play a role in the differentiation of myocytes, as ARPP expression was shown to be induced during the C2C12 differentiation in vitro. [19] A role for ARPP in regulating muscle gene expression and sensing stress signals was implicated in the finding that ARPP colocalizes with the transcriptional co-activator and co-repressor PML in myoblast nuclei, and binds p53 to enhance the p21(WAFI/CIPI) promoter. [20] It was further demonstrated that Nkx2.5 and p53 synergistically activate the ANKRD2 promoter to promote effects on myogenic differentiation. [21] At the sarcomere, ARPP binds titin at I-bands, which is potentiated by homo-dimerization and can alter the protein kinase A/protein kinase C phosphorylation status of itself or titin. [15] These studies demonstrate a stretch-responsive relationship between ARPP and Titin, which can be rapidly altered by post-translational mechanisms.

Functional insights into ARPP function have come from transgenic studies. In mice lacking all three muscle ankyrin repeat proteins (MARPs), ARPP, CARP, and DARP), skeletal muscles tended towards a more slower fiber type distribution, with longer resting sarcomere length, decreased fiber stiffness, expression of a longer titin isoform, greater degree of torque loss following eccentric contraction-related injury, and enhanced expression of MyoD and MLP. These findings suggest that ARPP and related MARP proteins may play a role in the passive stiffness and gene regulatory roles in skeletal muscle. [22] A study investigating ARPP function in cardiac muscle in which ARPP was knocked out alone or in combination with the other MARPs showed that mice displayed normal cardiac function at baseline and in response to pressure overload-induced cardiac hypertrophy, suggesting that these proteins are not essential for normal cardiac development or in response to a hypertrophic stimulus. [23]

ARPP has also shown to play a role in models of disease. ARPP has also exhibited elevated expression following skeletal muscle denervation, persisting for four weeks following the insult. [16] ARPP (ANKRD2) gene expression was also shown to be rapidly induced in a model of eccentric contraction-related injury, showing peak expression (6-11 times normal value) within 12–24 hours following injury, suggesting that ARPP may play a role in repair. [24] In a mouse model of muscular dystrophy with myositis (mdm) caused by a small deletion in titin, ANKRD2 mRNA expression was shown to be significantly elevated in skeletal muscle tissue along with that of CARP, suggesting a role for ARPP in titin-based signaling. [25] Levels of ARPP were also altered in a mouse model of diabetes. [26]

Clinical Significance

In patients with dilated cardiomyopathy, levels of ARPP were upregulated. [27]

ARPP expression patterns have been shown to be altered in patients with amyotrophic lateral sclerosis (ALS), with decreased expression in slow skeletal muscle fibers and increased expression in fast skeletal muscle fibers. [28]

ARPP has also been shown to be a potentially useful biomarker for the differential diagnosis between oncocytoma and chromophobe renal cell carcinomas. [29]

In non-pathologic physiology, ARPP mRNA expression in skeletal muscle of patients was shown to be elevated two days following fatiguing jumping exercises. Levels of CARP, MLP and calpain-2 mRNA levels were also enhanced, suggesting that these molecules may be part of a signaling network activated by physical exercise. [30]

Ankrd2 has been shown to be involved in the progression of some types of cancers, such as osteosarcoma [9] and head and neck squamous cell carcinoma. [10]

Interactions

ANKRD2 has been shown to interact with

Related Research Articles

<span class="mw-page-title-main">Titin</span> Largest-known protein in human muscles

Titin is a protein that in humans is encoded by the TTN gene. Titin is a giant protein, greater than 1 µm in length, that functions as a molecular spring that is responsible for the passive elasticity of muscle. It comprises 244 individually folded protein domains connected by unstructured peptide sequences. These domains unfold when the protein is stretched and refold when the tension is removed.

<span class="mw-page-title-main">Ankyrin repeat</span>

The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin tandem repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.

<span class="mw-page-title-main">Myomesin</span>

Myomesin is a protein family found in the M-line of the sarcomere structure. Myomesin has various forms throughout the body in striated muscles with specialized functions. This includes both slow and fast muscle fibers. Myomesin are made of 13 domains including a unique N-terminal followed by two immunoglobulin-like (Ig) domains, five fibronectin type III (Fn) domains, five more Ig domains. These domains all promote binding which indicates that myomesin is regulated through binding.

<span class="mw-page-title-main">Nebulette</span> Protein-coding gene in the species Homo sapiens

Nebulette is a cardiac-specific isoform belonging to the nebulin family of proteins. It is encoded by the NEBL gene. This family is composed of 5 members: nebulette, nebulin, N-RAP, LASP-1 and LASP-2. Nebulette localizes to Z-discs of cardiac muscle and appears to regulate the length of actin thin filaments.

<span class="mw-page-title-main">Alpha-actinin-2</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-2 is a protein which in humans is encoded by the ACTN2 gene. This gene encodes an alpha-actinin isoform that is expressed in both skeletal and cardiac muscles and functions to anchor myofibrillar actin thin filaments and titin to Z-discs.

<span class="mw-page-title-main">TPM2</span> Protein-coding gene in the species Homo sapiens

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

<span class="mw-page-title-main">Telethonin</span>

Telethonin, also known as Tcap, is a protein that in humans is encoded by the TCAP gene. Telethonin is expressed in cardiac and skeletal muscle at Z-discs and functions to regulate sarcomere assembly, T-tubule function and apoptosis. Telethonin has been implicated in several diseases, including limb-girdle muscular dystrophy, hypertrophic cardiomyopathy, dilated cardiomyopathy and idiopathic cardiomyopathy.

<span class="mw-page-title-main">TNNI2</span> Protein-coding gene in the species Homo sapiens

Troponin I, fast skeletal muscle is a protein that in humans is encoded by the TNNI2 gene.

<span class="mw-page-title-main">Obscurin</span> Protein-coding gene in the species Homo sapiens

Obscurin is a protein that in humans is encoded by the OBSCN gene. Obscurin belongs to the family of giant sarcomeric signaling proteins that includes titin and nebulin. Obscurin is expressed in cardiac and skeletal muscle, and plays a role in the organization of myofibrils during sarcomere assembly. A mutation in the OBSCN gene has been associated with hypertrophic cardiomyopathy and altered obscurin protein properties have been associated with other muscle diseases.

<span class="mw-page-title-main">ANKRD1</span> Protein-coding gene in the species Homo sapiens

Ankyrin repeat domain-containing protein 1, or Cardiac ankyrin repeat protein is a protein that in humans is encoded by the ANKRD1 gene also known as CARP. CARP is highly expressed in cardiac and skeletal muscle, and is a transcription factor involved in development and under conditions of stress. CARP has been implicated in several diseases, including dilated cardiomyopathy, hypertrophic cardiomyopathy, and several skeletal muscle myopathies.

<span class="mw-page-title-main">NRAP</span> Protein-coding gene in the species Homo sapiens

Nebulin-related-anchoring protein(N-RAP) is a protein that in humans is encoded by the NRAP gene. N-RAP is a muscle-specific isoform belonging to the nebulin family of proteins. This family is composed of 5 members: N-RAP, nebulin, nebulette, LASP-1 and LASP-2. N-RAP is involved in both myofibrillar myogenesis during development and cell-cell connections in mature muscle.

<span class="mw-page-title-main">TRIM63</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase TRIM63, also known as "MuRF1", is an enzyme that in humans is encoded by the TRIM63 gene.

<span class="mw-page-title-main">Myopalladin</span> Protein-coding gene in the species Homo sapiens

Myopalladin is a protein that in humans is encoded by the MYPN gene. Myopalladin is a muscle protein responsible for tethering proteins at the Z-disc and for communicating between the sarcomere and the nucleus in cardiac and skeletal muscle

<span class="mw-page-title-main">MYOM1</span> Protein-coding gene in humans

Myomesin-1 is a protein that in humans is encoded by the MYOM1 gene. Myomesin-1 is expressed in muscle cells and functions to stabilize the three-dimensional conformation of the thick filament. Embryonic forms of Myomesin-1 have been detected in dilated cardiomyopathy.

<span class="mw-page-title-main">ANKRD17</span> Protein-coding gene in the species Homo sapiens

Ankyrin repeat domain-containing protein 17 is a protein that in humans is encoded by the ANKRD17 gene.

<span class="mw-page-title-main">Ankyrin-1</span> Protein-coding gene in the species Homo sapiens

Ankyrin 1, also known as ANK-1, and erythrocyte ankyrin, is a protein that in humans is encoded by the ANK1 gene.

<span class="mw-page-title-main">ANKRD23</span> Protein-coding gene in the species Homo sapiens

Ankyrin repeat domain-containing protein 23 is a protein that in humans is encoded by the ANKRD23 gene.

<span class="mw-page-title-main">Myomesin-2</span> Protein-coding gene in the species Homo sapiens

Myomesin-2, also known as M-protein is a protein that in humans is encoded by the MYOM2 gene. M-protein is expressed in adult cardiac muscle and fast skeletal muscle, and functions to stabilize the three-dimensional arrangement of proteins comprising M-band structures in a sarcomere.

Ankyrin-2, also known as Ankyrin-B, and Brain ankyrin, is a protein which in humans is encoded by the ANK2 gene. Ankyrin-2 is ubiquitously expressed, but shows high expression in cardiac muscle. Ankyrin-2 plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in cardiomyocytes, as well as in costamere structures. Mutations in ANK2 cause a dominantly-inherited, cardiac arrhythmia syndrome known as long QT syndrome 4 as well as sick sinus syndrome; mutations have also been associated to a lesser degree with hypertrophic cardiomyopathy. Alterations in ankyrin-2 expression levels are observed in human heart failure.

<span class="mw-page-title-main">Ankyrin repeat domain 11</span> Protein-coding gene in the species Homo sapiens

Ankyrin repeat domain 11 is a protein that in humans is encoded by the ANKRD11 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000165887 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025172 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Kemp TJ, Sadusky TJ, Saltisi F, Carey N, Moss J, Yang SY, Sassoon DA, Goldspink G, Coulton GR (Sep 2000). "Identification of Ankrd2, a novel skeletal muscle gene coding for a stretch-responsive ankyrin-repeat protein". Genomics. 66 (3): 229–41. doi:10.1006/geno.2000.6213. PMID   10873377.
  6. 1 2 3 4 5 Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G (May 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". J. Mol. Biol. 339 (2): 313–25. doi:10.1016/j.jmb.2004.03.071. PMID   15136035.
  7. ↑ Mckoy G, Hou Y, Yang SY, Vega Avelaira D, Degens H, Goldspink G, Coulton GR (May 2005). "Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function". J. Appl. Physiol. 98 (6): 2337–43, discussion 2320. doi:10.1152/japplphysiol.01046.2004. PMID   15677738. S2CID   17104014.
  8. ↑ "Entrez Gene: ANKRD2 ankyrin repeat domain 2 (stretch responsive muscle)".
  9. 1 2 Piazzi M, Kojic S, Capanni C, Stamenkovic N, Bavelloni A, Marin O, Lattanzi G, Blalock W, Cenni V (January 2021). "Ectopic Expression of Ankrd2 Affects Proliferation, Motility and Clonogenic Potential of Human Osteosarcoma Cells". Cancers. 13 (2): 174. doi: 10.3390/cancers13020174 . PMC   7825408 . PMID   33419058.
  10. 1 2 Zhang LM, Su LX, Hu JZ, Wang M, Ju HY, Li X, Han YF, Xia WY, Guo W, Ren GX, Fan XD (October 2020). "Epigenetic regulation of VENTXP1 suppresses tumor proliferation via miR-205-5p/ANKRD2/NF-kB signaling in head and neck squamous cell carcinoma". Cell Death & Disease. 11 (10): 838. doi:10.1038/s41419-020-03057-w. PMC   7547684 . PMID   33037177.
  11. ↑ "Protein sequence of human ANKRD2 (Uniprot ID: Q9GZV1)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 26 June 2015. Retrieved 25 June 2015.
  12. ↑ "Protein sequence of human ANKRD2 (Uniprot ID: Q9GZV1-2)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 2015-06-26. Retrieved 2015-06-25.
  13. 1 2 Pallavicini A, Kojić S, Bean C, Vainzof M, Salamon M, Ievolella C, Bortoletto G, Pacchioni B, Zatz M, Lanfranchi G, Faulkner G, Valle G (Jul 2001). "Characterization of human skeletal muscle Ankrd2". Biochemical and Biophysical Research Communications. 285 (2): 378–86. doi:10.1006/bbrc.2001.5131. PMID   11444853.
  14. 1 2 Moriyama M, Tsukamoto Y, Fujiwara M, Kondo G, Nakada C, Baba T, Ishiguro N, Miyazaki A, Nakamura K, Hori N, Sato K, Shomori K, Takeuchi K, Satoh H, Mori S, Ito H (Jul 2001). "Identification of a novel human ankyrin-repeated protein homologous to CARP". Biochemical and Biophysical Research Communications. 285 (3): 715–23. doi:10.1006/bbrc.2001.5216. PMID   11453652.
  15. 1 2 Lun AS, Chen J, Lange S (Sep 2014). "Probing muscle ankyrin-repeat protein (MARP) structure and function". Anatomical Record. 297 (9): 1615–29. doi:10.1002/ar.22968. PMC   4135402 . PMID   25125175.
  16. 1 2 3 Tsukamoto Y, Senda T, Nakano T, Nakada C, Hida T, Ishiguro N, Kondo G, Baba T, Sato K, Osaki M, Mori S, Ito H, Moriyama M (May 2002). "Arpp, a new homolog of carp, is preferentially expressed in type 1 skeletal muscle fibers and is markedly induced by denervation". Laboratory Investigation. 82 (5): 645–55. doi: 10.1038/labinvest.3780459 . PMID   12004005.
  17. ↑ Jasnic-Savovic J, Nestorovic A, Savic S, Karasek S, Vitulo N, Valle G, Faulkner G, Radojkovic D, Kojic S (Jun 2015). "Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes". Histochemistry and Cell Biology. 143 (6): 583–97. doi:10.1007/s00418-015-1307-5. PMID   25585647. S2CID   5174178.
  18. ↑ Wang L, Lei M, Xiong Y (Apr 2011). "Molecular characterization and different expression patterns of the muscle ankyrin repeat protein (MARP) family during porcine skeletal muscle development in vitro and in vivo". Animal Biotechnology. 22 (2): 87–99. doi:10.1080/10495398.2011.559562. PMID   21500110. S2CID   26069450.
  19. 1 2 Ishiguro N, Baba T, Ishida T, Takeuchi K, Osaki M, Araki N, Okada E, Takahashi S, Saito M, Watanabe M, Nakada C, Tsukamoto Y, Sato K, Ito K, Fukayama M, Mori S, Ito H, Moriyama M (May 2002). "Carp, a cardiac ankyrin-repeated protein, and its new homologue, Arpp, are differentially expressed in heart, skeletal muscle, and rhabdomyosarcomas". The American Journal of Pathology. 160 (5): 1767–78. doi:10.1016/S0002-9440(10)61123-6. PMC   1850855 . PMID   12000728.
  20. ↑ Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G (May 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". Journal of Molecular Biology. 339 (2): 313–25. doi:10.1016/j.jmb.2004.03.071. PMID   15136035.
  21. ↑ Kojic S, Nestorovic A, Rakicevic L, Protic O, Jasnic-Savovic J, Faulkner G, Radojkovic D (Mar 2015). "Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity". Archives of Biochemistry and Biophysics. 569: 45–53. doi:10.1016/j.abb.2015.02.001. PMID   25677450.
  22. ↑ Barash IA, Bang ML, Mathew L, Greaser ML, Chen J, Lieber RL (Jul 2007). "Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle". American Journal of Physiology. Cell Physiology. 293 (1): C218–27. doi:10.1152/ajpcell.00055.2007. PMID   17392382. S2CID   29659381.
  23. ↑ Bang ML, Gu Y, Dalton ND, Peterson KL, Chien KR, Chen J (2014). "The muscle ankyrin repeat proteins CARP, Ankrd2, and DARP are not essential for normal cardiac development and function at basal conditions and in response to pressure overload". PLOS ONE. 9 (4): e93638. Bibcode:2014PLoSO...993638B. doi: 10.1371/journal.pone.0093638 . PMC   3988038 . PMID   24736439.
  24. ↑ Barash IA, Mathew L, Ryan AF, Chen J, Lieber RL (Feb 2004). "Rapid muscle-specific gene expression changes after a single bout of eccentric contractions in the mouse". American Journal of Physiology. Cell Physiology. 286 (2): C355–64. doi:10.1152/ajpcell.00211.2003. PMID   14561590.
  25. ↑ Witt CC, Ono Y, Puschmann E, McNabb M, Wu Y, Gotthardt M, Witt SH, Haak M, Labeit D, Gregorio CC, Sorimachi H, Granzier H, Labeit S (Feb 2004). "Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling". Journal of Molecular Biology. 336 (1): 145–54. doi:10.1016/j.jmb.2003.12.021. PMID   14741210.
  26. ↑ Lehti TM, Silvennoinen M, Kivelä R, Kainulainen H, Komulainen J (Feb 2007). "Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle". American Journal of Physiology. Endocrinology and Metabolism. 292 (2): E533–42. doi:10.1152/ajpendo.00229.2006. PMID   17003243. S2CID   23964462.
  27. ↑ Nagueh SF, Shah G, Wu Y, Torre-Amione G, King NM, Lahmers S, Witt CC, Becker K, Labeit S, Granzier HL (Jul 2004). "Altered titin expression, myocardial stiffness, and left ventricular function in patients with dilated cardiomyopathy". Circulation. 110 (2): 155–62. doi: 10.1161/01.CIR.0000135591.37759.AF . PMID   15238456.
  28. ↑ Nakamura K, Nakada C, Takeuchi K, Osaki M, Shomori K, Kato S, Ohama E, Sato K, Fukayama M, Mori S, Ito H, Moriyama M (2002). "Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich region, in atrophic muscles in amyotrophic lateral sclerosis". Pathobiology. 70 (4): 197–203. doi:10.1159/000069329. PMID   12679596. S2CID   37199318.
  29. ↑ Shomori K, Nagashima Y, Kuroda N, Honjo A, Tsukamoto Y, Tokuyasu N, Maeta N, Matsuura K, Hijiya N, Yano S, Yokoyama S, Ito H, Moriyama M (Feb 2007). "ARPP protein is selectively expressed in renal oncocytoma, but rarely in renal cell carcinomas". Modern Pathology. 20 (2): 199–207. doi: 10.1038/modpathol.3800730 . PMID   17206105.
  30. ↑ Lehti M, Kivelä R, Komi P, Komulainen J, Kainulainen H, Kyröläinen H (Apr 2009). "Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains". Journal of Applied Physiology. 106 (4): 1419–24. doi:10.1152/japplphysiol.90660.2008. PMID   19150862. S2CID   15423940.
  31. ↑ Miller MK, Bang ML, Witt CC, Labeit D, Trombitas C, Watanabe K, Granzier H, McElhinny AS, Gregorio CC, Labeit S (Nov 2003). "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules". Journal of Molecular Biology. 333 (5): 951–64. doi:10.1016/j.jmb.2003.09.012. PMID   14583192.
  32. ↑ PMID 28531892
  33. ↑ Cenni V, Bavelloni A, Beretti F, Tagliavini F, Manzoli L, Lattanzi G, Maraldi NM, Cocco L, Marmiroli S (August 2011). "Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2)O(2)". Molecular Biology of the Cell. 22 (16): 2946–56. doi:10.1091/mbc.E10-11-0928. PMC   3154889 . PMID   21737686.

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