Proteomics

Dataset Information

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HAX1-interactome in cervical cancer cell line (HeLa)


ABSTRACT: HAX1 is a 32-kDa protein of unknown structure, involved in the regulation of apoptosis, cell migration and calcium homeostasis. It was also shown to bind mRNA. Scarcity of structural elements and the presence of a disordered region, inferred from HAX1 sequence, suggests that HAX1 is intrinsically disordered, and may have many protein-protein interactions. So far about 40 different proteins were characterized as HAX1 protein partners. In the present work, applying immunoaffinity chromatography coupled with mass spectrometry, we identified new candidates for HAX1 binding partners in cervical carcinoma cells. More than a half of these newly identified proteins represent RNA-binding proteins. There is also a big group of proteins, mostly mitochondrial, involved in cellular metabolism. These results imply that HAX1 has more protein partners than hitherto described. Subsequent analysis of these interactions may shed some light into molecular mechanisms of HAX1 functions, especially its involvement in mRNA processing and its role in protection against oxidative stress.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Tymon Rubel  

LAB HEAD: Ewa Grzybowska

PROVIDER: PXD007887 | Pride | 2020-11-11

REPOSITORIES: Pride

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Publications

The interactome of multifunctional HAX1 protein suggests its role in the regulation of energy metabolism, de-aggregation, cytoskeleton organization and RNA-processing.

Wakula Maciej M   Balcerak Anna A   Rubel Tymon T   Chmielarczyk Mateusz M   Konopinski Ryszard R   Lyczek Filip F   Grzybowska Ewa A EA  

Bioscience reports 20201101 11


HCLS1-associated protein X-1 (HAX1) is a multifunctional protein involved in many cellular processes, including apoptosis, cell migration and calcium homeostasis, but its mode of action still remains obscure. Multiple HAX1 protein partners have been identified, but they are involved in many distinct pathways, form different complexes and do not constitute a coherent group. By characterizing HAX1 protein interactome using targeted approach, we attempt to explain HAX1 multiple functions and its ro  ...[more]

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