Dataset Information

Analysis of Zyxin's interactome and phosphosites in early Xenopus laevis development by Data-Independent Acquisition proteomics

ABSTRACT: Protein complexes are key players in development, functioning as molecular machines whose proper assembly is crucial for numerous cellular processes. Their formation at the correct time and location is facilitated by specialized scaffold proteins. A prominent example is the mechanosensitive cytoskeletal protein zyxin. Zyxin is of particular interest due to its role in assembling actin filaments within focal adhesion complexes and transducing signals from the cytoskeleton to the genetic apparatus. In this study, we employed co-immunoprecipitation coupled with mass spectrometry to analyze changes in zyxin-associated protein complexes from lysates of Xenopus frog embryos across three early developmental stages: early gastrulation, early neurulation, and late neural fold stages. Our analysis revealed stage-specific alterations in the isoform repertoires of several established zyxin partners, including components of the focal adhesion complex, transcriptional regulators, and proteins involved in its phosphorylation. We also identified changes in the phosphorylation patterns of different zyxin isoforms. Collectively, these findings provide a valuable resource for elucidating the function of the scaffold protein zyxin and its role in embryonic tissue development. Furthermore, the identification of kinases and caspases within the zyxin interactome suggests its involvement in key signaling pathways related to cell survival and apoptosis. Finally, confirmed interactions with partners such as 14-3-3 proteins, Yap, and TEF-1 highlight the multifaceted role of zyxin in cellular regulation and its potential as a therapeutic target.

INSTRUMENT(S):

ORGANISM(S): Xenopus Laevis (african Clawed Frog)

TISSUE(S): Embryo

SUBMITTER: Rustam Ziganshin

LAB HEAD: Zaraisky A.G.

PROVIDER: PXD071213 | Pride | 2026-02-02

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	NMart_20251004_091_RZ_CTRL-14.raw	Raw
	NMart_20251004_093_RZ_CTRL-16.raw	Raw
	NMart_20251004_095_RZ_Z-14.raw	Raw
	NMart_20251004_097_RZ_Z-16.raw	Raw
	NMart_20251010_100_RZ_CTRL-10.raw	Raw

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Publications

Co-Immunoprecipitation-Coupled Mass Spectrometry Analysis of Zyxin's Interactome and Phosphosites in Early <i>Xenopus laevis</i> Development.

Parshina Elena A EA Ziganshin Rustam H RH Zaraisky Andrey G AG Martynova Natalia Y NY

International journal of molecular sciences 20260111 2

Protein complexes, assembled by scaffold proteins, act as molecular machines driving development. The mechanosensitive adapter protein Zyxin is a key example, integrating actin cytoskeleton dynamics with gene expression. However, the developmental regulation of its interactions and post-translational modifications remains poorly understood. Here, we characterize the dynamic Zyxin interactome across three early developmental stages of <i>Xenopus laevis</i> (from gastrulation to neurulation) using ...[more]

PMID: 41596386

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