SYNPO2

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SYNPO2
Identifiers
Aliases SYNPO2
External IDs MGI: 2153070 HomoloGene: 15400 GeneCards: SYNPO2
Genetically Related Diseases
amyotrophic lateral sclerosis[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001128933
NM_001128934
NM_001286754
NM_001286755
NM_133477

NM_080451

RefSeq (protein)

NP_001122405
NP_001122406
NP_001273683
NP_001273684
NP_597734

NP_536699

Location (UCSC) Chr 4: 118.85 – 119.06 Mb Chr 3: 123.08 – 123.24 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Myopodin protein, also called Synaptopodin-2 is a protein that in humans is encoded by the SYNPO2 gene.[4][5][6] Myopodin is expressed in cardiac, smooth muscle and skeletal muscle, and localizes to Z-disc structures.

Structure[edit]

Myopodin is a 117.4 kDa protein composed of 1093 amino acids,[7] although four alternatively-spliced isoforms have been described.[8] Myopodin contains one PPXY motif, multiple PXXP motifs, and two potential nuclear localization sequences (one N-terminal and one C-terminal).[4] PPXY motifs have been shown to mediate interactions, and PXXP motifs represent potential sites of interaction for SH3 domain-containing proteins. Myopodin contains a novel actin binding site (between amino acids 410 and 563) in the center of the protein.[4]

Function[edit]

During myotube differentiation, myopodin interacts with stress fibers prior to co-localizing with alpha actinin-2 at Z-discs in mature striated muscle cells.[4] Myopodin has been shown to shuttle between the nucleus and cytoplasm in myoblasts and myotubes in response to stress; its export from the nucleus is sensitive to lemtomycin B.[4] The nuclear localization of myopodin is sensitive to Importin 13, which directly binds myopodin and facilitates its translocation.[9] Importin binding and nuclear import of myopodin appears to be mediated by serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3 beta [10] Myopodin appears to regulate compartmentalized, intracellular signal transduction between the Z-disc and nucleus in cardiac muscle cells, by forming a Z-disc signaling complex with alpha actinin-2, calcineurin, CaMKII, muscle-specific A-kinase anchoring protein, and myomegalin.[11] Specifically, phosphorylation by protein kinase A or CaMKII, and dephosphorylation by calcineurin facilitates the binding or release, respectively, of 14-3-3-beta, and the corresponding nuclear or cytoplasmic localization, respectively, of myopodin.[11]

Interactions[edit]

Myopodin interacts with:

References[edit]

  1. ^ "Diseases that are genetically associated with SYNPO2 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ a b c d e f g Weins A, Schwarz K, Faul C, Barisoni L, Linke WA, Mundel P (Oct 2001). "Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein". The Journal of Cell Biology. 155 (3): 393–404. doi:10.1083/jcb.200012039. PMC 2150840Freely accessible. PMID 11673475. 
  5. ^ Liang J, Ke G, You W, Peng Z, Lan J, Kalesse M, Tartakoff AM, Kaplan F, Tao T (Jan 2008). "Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin". Molecular and Cellular Biochemistry. 307 (1–2): 93–100. doi:10.1007/s11010-007-9588-1. PMID 17828378. 
  6. ^ "Entrez Gene: SYNPO2 synaptopodin 2". 
  7. ^ Joon-Sub Chung. "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information". heartproteome.org. 
  8. ^ "SYNPO2 - Synaptopodin-2 - Homo sapiens (Human) - SYNPO2 gene & protein". uniprot.org. 
  9. ^ a b Liang J, Ke G, You W, Peng Z, Lan J, Kalesse M, Tartakoff AM, Kaplan F, Tao T (Jan 2008). "Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin". Molecular and Cellular Biochemistry. 307 (1–2): 93–100. doi:10.1007/s11010-007-9588-1. PMID 17828378. 
  10. ^ Faul C, Hüttelmaier S, Oh J, Hachet V, Singer RH, Mundel P (May 2005). "Promotion of importin alpha-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3". The Journal of Cell Biology. 169 (3): 415–24. doi:10.1083/jcb.200411169. PMC 2171942Freely accessible. PMID 15883195. 
  11. ^ a b c d e f Faul C, Dhume A, Schecter AD, Mundel P (Dec 2007). "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes". Molecular and Cellular Biology. 27 (23): 8215–27. doi:10.1128/MCB.00950-07. PMC 2169179Freely accessible. PMID 17923693. 

Further reading[edit]