SYNPO2: Difference between revisions

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== Structure ==
== Structure ==


Myopodin is a 117.4 kDa protein composed of 1093 amino acids,<ref>{{cite web|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=Q9UMS6|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information|author=Joon-Sub Chung|work=heartproteome.org}}</ref> although four alternatively-spliced isoforms have been described.<ref>{{cite web|url=http://www.uniprot.org/uniprot/Q9UMS6|title=SYNPO2 - Synaptopodin-2 - Homo sapiens (Human) - SYNPO2 gene & protein|work=uniprot.org}}</ref> Myopodin contains one PPXY motif, multiple PXXP motifs, and two potential [[nuclear localization sequence]]s (one [[N-terminus|N-terminal]] and one [[C-terminus|C-terminal]]).<ref name="pmid11673475" /> PPXY motifs have been shown to mediate [[protein–protein interactions|interactions]], and PXXP motifs represent potential sites of [[protein-protein interaction|interaction]] for [[SH3 domain]]-containing proteins. Myopodin contains a novel [[ACTC1|actin]] binding site (between amino acids 410 and 563) in the center of the protein.<ref name="pmid11673475" />
Myopodin is a 117.4 kDa protein composed of 1093 amino acids,<ref>{{cite web|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=Q9UMS6|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information|author=Joon-Sub Chung|work=heartproteome.org}}</ref> although four alternatively-spliced isoforms have been described.<ref>{{cite web|url=https://www.uniprot.org/uniprot/Q9UMS6|title=SYNPO2 - Synaptopodin-2 - Homo sapiens (Human) - SYNPO2 gene & protein|work=uniprot.org}}</ref> Myopodin contains one PPXY motif, multiple PXXP motifs, and two potential [[nuclear localization sequence]]s (one [[N-terminus|N-terminal]] and one [[C-terminus|C-terminal]]).<ref name="pmid11673475" /> PPXY motifs have been shown to mediate [[protein–protein interactions|interactions]], and PXXP motifs represent potential sites of [[protein-protein interaction|interaction]] for [[SH3 domain]]-containing proteins. Myopodin contains a novel [[ACTC1|actin]] binding site (between amino acids 410 and 563) in the center of the protein.<ref name="pmid11673475" />


== Function ==
== Function ==

Revision as of 06:45, 23 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Myopodin protein, also called Synaptopodin-2 is a protein that in humans is encoded by the SYNPO2 gene.[1][2][3] Myopodin is expressed in cardiac, smooth muscle and skeletal muscle, and localizes to Z-disc structures.

Structure

Myopodin is a 117.4 kDa protein composed of 1093 amino acids,[4] although four alternatively-spliced isoforms have been described.[5] Myopodin contains one PPXY motif, multiple PXXP motifs, and two potential nuclear localization sequences (one N-terminal and one C-terminal).[1] 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.[1]

Function

During myotube differentiation, myopodin interacts with stress fibers prior to co-localizing with alpha actinin-2 at Z-discs in mature striated muscle cells.[1] 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.[1] The nuclear localization of myopodin is sensitive to Importin 13, which directly binds myopodin and facilitates its translocation.[6] Importin binding and nuclear import of myopodin appears to be mediated by serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3 beta [7] 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.[8] 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.[8]

Interactions

Myopodin interacts with:

References

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 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 2150840. PMID 11673475.
  2. 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.
  3. "Entrez Gene: SYNPO2 synaptopodin 2".
  4. Joon-Sub Chung. "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information". heartproteome.org.
  5. "SYNPO2 - Synaptopodin-2 - Homo sapiens (Human) - SYNPO2 gene & protein". uniprot.org.
  6. 6.0 6.1 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.
  7. 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 2171942. PMID 15883195.
  8. 8.0 8.1 8.2 8.3 8.4 8.5 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 2169179. PMID 17923693.

Further reading