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1.
Sci Rep ; 8(1): 17785, 2018 Dec 07.
Artigo em Inglês | MEDLINE | ID: mdl-30531996

RESUMO

A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.

2.
Biochim Biophys Acta Mol Cell Res ; 1865(2): 406-420, 2018 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-29175376

RESUMO

ß-Dystroglycan (ß-DG) is a plasma membrane protein that has ability to target to the nuclear envelope (NE) to maintain nuclear architecture. Nevertheless, mechanisms controlling ß-DG nuclear localization and the physiological consequences of a failure of trafficking are largely unknown. We show that ß-DG has a nuclear export pathway in myoblasts that depends on the recognition of a nuclear export signal located in its transmembrane domain, by CRM1. Remarkably, NES mutations forced ß-DG nuclear accumulation resulting in mislocalization and decreased levels of emerin and lamin B1 and disruption of various nuclear processes in which emerin (centrosome-nucleus linkage and ß-catenin transcriptional activity) and lamin B1 (cell cycle progression and nucleoli structure) are critically involved. In addition to nuclear export, the lifespan of nuclear ß-DG is restricted by its nuclear proteasomal degradation. Collectively our data show that control of nuclear ß-DG content by the combination of CRM1 nuclear export and nuclear proteasome pathways is physiologically relevant to preserve proper NE structure and activity.


Assuntos
Distroglicanas/metabolismo , Carioferinas/metabolismo , Laminina/metabolismo , Membrana Nuclear/metabolismo , Complexo de Endopeptidases do Proteassoma/metabolismo , Proteólise , Receptores Citoplasmáticos e Nucleares/metabolismo , Animais , Linhagem Celular , Distroglicanas/genética , Carioferinas/genética , Laminina/genética , Camundongos , Membrana Nuclear/genética , Complexo de Endopeptidases do Proteassoma/genética , Receptores Citoplasmáticos e Nucleares/genética , Proteína Exportina 1
3.
Sci Rep ; 7(1): 9906, 2017 08 29.
Artigo em Inglês | MEDLINE | ID: mdl-28852008

RESUMO

ß-Dystroglycan (ß-DG) is a transmembrane protein with critical roles in cell adhesion, cytoskeleton remodeling and nuclear architecture. This functional diversity is attributed to the ability of ß-DG to target to, and conform specific protein assemblies at the plasma membrane (PM) and nuclear envelope (NE). Although a classical NLS and importin α/ß mediated nuclear import pathway has already been described for ß-DG, the intracellular trafficking route by which ß-DG reaches the nucleus is unknown. In this study, we demonstrated that ß-DG undergoes retrograde intracellular trafficking from the PM to the nucleus via the endosome-ER network. Furthermore, we provided evidence indicating that the translocon complex Sec61 mediates the release of ß-DG from the ER membrane, making it accessible for importins and nuclear import. Finally, we show that phosphorylation of ß-DG at Tyr890 is a key stimulus for ß-DG nuclear translocation. Collectively our data describe the retrograde intracellular trafficking route that ß-DG follows from PM to the nucleus. This dual role for a cell adhesion receptor permits the cell to functionally connect the PM with the nucleus and represents to our knowledge the first example of a cell adhesion receptor exhibiting retrograde nuclear trafficking and having dual roles in PM and NE.

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