p53-cofactor JMY is a multifunctional actin nucleation factor.
Many cellular structures are assembled from networks of actin filaments, and the architecture of these networks depends on the mechanism by which the filaments are formed. Several classes of proteins are known to assemble new filaments, including the Arp2/3 complex, which creates branched filament n...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2009
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| _version_ | 1797074153152446464 |
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| author | Zuchero, J Coutts, A Quinlan, M Thangue, N Mullins, R |
| author_facet | Zuchero, J Coutts, A Quinlan, M Thangue, N Mullins, R |
| author_sort | Zuchero, J |
| collection | OXFORD |
| description | Many cellular structures are assembled from networks of actin filaments, and the architecture of these networks depends on the mechanism by which the filaments are formed. Several classes of proteins are known to assemble new filaments, including the Arp2/3 complex, which creates branched filament networks, and Spire, which creates unbranched filaments. We find that JMY, a vertebrate protein first identified as a transcriptional co-activator of p53, combines these two nucleating activities by both activating Arp2/3 and assembling filaments directly using a Spire-like mechanism. Increased levels of JMY expression enhance motility, whereas loss of JMY slows cell migration. When slowly migrating HL-60 cells are differentiated into highly motile neutrophil-like cells, JMY moves from the nucleus to the cytoplasm and is concentrated at the leading edge. Thus, JMY represents a new class of multifunctional actin assembly factor whose activity is regulated, at least in part, by sequestration in the nucleus. |
| first_indexed | 2024-03-06T23:32:14Z |
| format | Journal article |
| id | oxford-uuid:6c70f11b-de4c-4193-b3c4-34348c8e8afe |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:32:14Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:6c70f11b-de4c-4193-b3c4-34348c8e8afe2022-03-26T19:10:51Zp53-cofactor JMY is a multifunctional actin nucleation factor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6c70f11b-de4c-4193-b3c4-34348c8e8afeEnglishSymplectic Elements at Oxford2009Zuchero, JCoutts, AQuinlan, MThangue, NMullins, RMany cellular structures are assembled from networks of actin filaments, and the architecture of these networks depends on the mechanism by which the filaments are formed. Several classes of proteins are known to assemble new filaments, including the Arp2/3 complex, which creates branched filament networks, and Spire, which creates unbranched filaments. We find that JMY, a vertebrate protein first identified as a transcriptional co-activator of p53, combines these two nucleating activities by both activating Arp2/3 and assembling filaments directly using a Spire-like mechanism. Increased levels of JMY expression enhance motility, whereas loss of JMY slows cell migration. When slowly migrating HL-60 cells are differentiated into highly motile neutrophil-like cells, JMY moves from the nucleus to the cytoplasm and is concentrated at the leading edge. Thus, JMY represents a new class of multifunctional actin assembly factor whose activity is regulated, at least in part, by sequestration in the nucleus. |
| spellingShingle | Zuchero, J Coutts, A Quinlan, M Thangue, N Mullins, R p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title | p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title_full | p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title_fullStr | p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title_full_unstemmed | p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title_short | p53-cofactor JMY is a multifunctional actin nucleation factor. |
| title_sort | p53 cofactor jmy is a multifunctional actin nucleation factor |
| work_keys_str_mv | AT zucheroj p53cofactorjmyisamultifunctionalactinnucleationfactor AT couttsa p53cofactorjmyisamultifunctionalactinnucleationfactor AT quinlanm p53cofactorjmyisamultifunctionalactinnucleationfactor AT thanguen p53cofactorjmyisamultifunctionalactinnucleationfactor AT mullinsr p53cofactorjmyisamultifunctionalactinnucleationfactor |