Proteomics

Dataset Information

0

ZO-1 phosphorylation upon ERK activation


ABSTRACT: This dataset was generated to identify phosphorylation sites of ZO-1 regulated by ERK signaling. Cells were treated with TPA alone or with TPA in combination with the MEK inhibitor PD0325901, followed by phosphopeptide enrichment and LC–MS/MS analysis. TPA activates multiple kinases including ERK, whereas PD0325901 selectively inhibits MEK, the upstream activator of ERK. Thus, ERK activity is specifically suppressed in the co-treated condition. Phosphorylation sites detected in the TPA-treated samples but not in the TPA + PD0325901-treated samples are considered to be associated with ERK-dependent phosphorylation of ZO-1.

INSTRUMENT(S):

ORGANISM(S): Canis Familiaris (dog) (canis Lupus Familiaris)

TISSUE(S): Epithelial Cell, Kidney

SUBMITTER: Sayuki Hirano  

LAB HEAD: Kazuhiro Aoki

PROVIDER: PXD076445 | Pride | 2026-04-17

REPOSITORIES: Pride

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Publications

ZO-1 shuttles between apical junctional complexes and podosomes by riding ERK activation waves.

Hirano Sayuki S   Kondo Yohei Y   Kitajima Asayuki A   Kinoshita Noriyuki N   Otani Tetsuhisa T   Furuse Mikio M   Ueno Naoto N   Aoki Kazuhiro K  

Nature communications 20260509 1


Collective cell migration is essential in various physiological processes, including embryonic development, wound healing, and cancer metastasis. However, the mechanisms by which individual cells achieve coordinated movement remain elusive. Here, we demonstrate that zonula occludens-1 (ZO-1), a scaffolding protein of tight junctions (TJs), dynamically translocates to form cell-extracellular matrix (ECM) adhesion complexes, podosomes, at the basal cell surface during migration. Extracellular sign  ...[more]

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