Abstract:
:LASP-1 is a multidomain protein predominantly localized at focal contacts, where it regulates cytoskeleton dynamics and cell migration. However, in different tumor entities, a nuclear LASP-1 accumulation is observed, thought to have an important role in cancer progression. Until now, the molecular mechanisms that control LASP-1 nuclear import were not elucidated. Here, we identified a novel LASP-1-binding partner, zona occludens protein 2 (ZO-2), and established its role in the signal transduction pathway of LASP-1 nucleo-cytoplasmatic shuttling. Phosphorylation of LASP-1 by PKA at serine 146 induces translocation of the LASP-1/ZO-2 complex from the cytoplasm to the nucleus. Interaction occurs within the carboxyterminal proline-rich motif of ZO-2 and the SH3 domain in LASP-1. In situ proximity ligation assay confirmed the direct binding between LASP-1 and ZO-2 and visualized the shuttling. Nuclear export is mediated by Crm-1 and a newly identified nuclear export signal in LASP-1. Finally, dephosphorylation of LASP-1 by phosphatase PP2B is suggested to relocalize the protein back to focal contacts. In summary, we define a new pathway for LASP-1 in tumor progression.
journal_name
Oncogenejournal_title
Oncogeneauthors
Mihlan S,Reiß C,Thalheimer P,Herterich S,Gaetzner S,Kremerskothen J,Pavenstädt HJ,Lewandrowski U,Sickmann A,Butt Edoi
10.1038/onc.2012.216subject
Has Abstractpub_date
2013-04-18 00:00:00pages
2107-13issue
16eissn
0950-9232issn
1476-5594pii
onc2012216journal_volume
32pub_type
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