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Data · dataset · 2015

Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin

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Altered phosphorylation status of the C-terminal Thr residues of Ezrin/Radixin/Moesin (ERM) is often linked to cell shape change.

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To determine the role of phophorylated ERM, we modified phosphorylation status of ERM and investigated changes in cell adhesion and morphology. Treatment with Calyculin-A (Cal-A), a protein phosphatase inhibitor, dramatically augmented phosphorylated ERM (phospho-ERM).

Cal-A-treatment or expression of phospho-mimetic Moesin mutant (Moesin-TD) induced cell rounding in adherent cells. Moreover, reattachment of detached cells to substrate was inhibited by either treatment. Phospho-ERM, Moesin-TD and actin cytoskeleton were observed at the plasma membrane of such round cells.

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Augmented cell surface rigidity was also observed in both cases.Meanwhile, non-adherent KG-1 cells were rather rich in phospho-ERM. Treatment with Staurosporine, a protein kinase inhibitor that dephosphorylates phospho-ERM, up-regulated the integrin-dependent adhesion of KG-1 cells to substrate.These findings strongly suggest the followings: (1) Phospho-ERM inhibit cell adhesion, and therefore, dephosphorylation of ERM proteins is essential for cell adhesion.

(2) Phospho-ERM induce formation and/or maintenance of spherical cell shape. (3) ERM are constitutively both phosphorylated and dephosphorylated in cultured adherent and non-adherent cells.

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Cancer · Physics
Provenance · 1 source records, 13 field assertions
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DataCite10.6084/m9.figshare.162192213 d agoJSON v1
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concepts[disease].local:disease:cancermapping · DataCitevocabulary-mapper@1.0.0keywords['Cancer']
concepts[field].fos:biological-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:clinical-medicinesource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:health-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].local:field:physicsmapping · DataCitevocabulary-mapper@1.0.0keywords['Physics']
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