Proteomics

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Data-Independent Acquisition-Based global phosphoproteomics reveals diverse roles of AELs (Arabidopsis EL1-like) Casein kinase 1 in plant development


ABSTRACT: Casein kinase 1 (CK1) is a highly conserved and ubiquitous serine/threonine protein kinase in eukaryotic cells. AELs (Arabidopsis EL1-like) are plant-specific CK1s and function in a wide range of physiological and signaling processes. To comprehensively understand the cellular functions and regulatory mechanism of AELs-mediated phosphorylation, we conducted a quantitative data-independent acquisition (DIA) based phosphoproteomic assay. A total of 3107 phosphopeptides and 1032 putative substrates were detected and enriched novel phosphorylation motifs were identified, which greatly expanded the candidate substrates and functions of CK1, as well as those from human and rice.

ORGANISM(S): Arabidopsis Thaliana

SUBMITTER: Hongwei Xue  

PROVIDER: PXD035098 | iProX | Tue Jul 05 00:00:00 GMT+01:00 2022

REPOSITORIES: iProX

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Data-independent acquisition-based global phosphoproteomics reveal the diverse roles of casein kinase 1 in plant development.

Qu Li L   Liu Moyang M   Zheng Lingli L   Wang Xu X   Xue Hongwei H  

Science bulletin 20230809 18


Casein kinase 1 (CK1) is serine/threonine protein kinase highly conserved among eukaryotes, and regulates multiple developmental and signaling events through phosphorylation of target proteins. Arabidopsis early flowering 1 (EL1)-like (AELs) are plant-specific CK1s with varied functions, but identification and validation of their substrates is a major bottleneck in elucidating their physiological roles. Here, we conducted a quantitative phosphoproteomic analysis in data-independent acquisition m  ...[more]

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