Coiled-Coil Domain Containing Protein 124 Is a Novel Centrosome and Midbody Protein That Interacts with the Ras-Guanine Nucleotide Exchange Factor 1B and Is Involved in Cytokinesis

Telkoparan, Pelin; Erkek, Serap; Yaman, Elif; Alotaibi, Hani; Bayık, Defne; Tazebay, Uygar Halis

doi:10.1371/journal.pone.0069289

Cited by 22 publications

(28 citation statements)

References 51 publications

(73 reference statements)

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“…We identified putative orthologs of yeast Lso2 in multiple eukaryotes, suggesting a conserved function. The human ortholog of Lso2, CCDC124, is a poorly characterized protein suggested to localize to the midbody during cytokinesis in HeLa cells [ 53 ] and to interact with Protein Kinase R during innate immune stimulation of HEK293 cells [ 54 ]. CCDC124 was independently predicted to contain a coiled-coil domain at its N-terminus ( Fig 3A ) [ 37 , 38 ] and is ubiquitously expressed across two dozen human tissues profiled by proteomics [ 55 ].…”

Section: Resultsmentioning

confidence: 99%

Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

et al. 2018

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Ribosome-binding proteins function broadly in protein synthesis, gene regulation, and cellular homeostasis, but the complete complement of functional ribosome-bound proteins remains unknown. Using quantitative mass spectrometry, we identified late-annotated short open reading frame 2 (Lso2) as a ribosome-associated protein that is broadly conserved in eukaryotes. Genome-wide crosslinking and immunoprecipitation of Lso2 and its human ortholog coiled-coil domain containing 124 (CCDC124) recovered 25S ribosomal RNA in a region near the A site that overlaps the GTPase activation center. Consistent with this location, Lso2 also crosslinked to most tRNAs. Ribosome profiling of yeast lacking LSO2 (lso2Δ) revealed global translation defects during recovery from stationary phase with translation of most genes reduced more than 4-fold. Ribosomes accumulated at start codons, were depleted from stop codons, and showed codon-specific changes in occupancy in lso2Δ. These defects, and the conservation of the specific ribosome-binding activity of Lso2/CCDC124, indicate broadly important functions in translation and physiology.

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Section: Resultsmentioning

confidence: 99%

Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

et al. 2018

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“…Previously described as a family of unknown proteins named DUF1014 (IPR010422), there has been a recent report of a human member of this family, Ccdc124 (Coiled-Coil Domain Containing Protein 124), identified as a novel component of the centrosome during interphase and G2/M transition and is involved in cytokinesis (24). …”

Section: Resultsmentioning

confidence: 99%

A Pap1–Oxs1 signaling pathway for disulfide stress inSchizosaccharomyces pombe

He¹,

Chen²,

Song³

et al. 2016

Nucleic Acids Res

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We describe a Pap1–Oxs1 pathway for diamide-induced disulfide stress in Schizosaccharomyces pombe, where the nucleocytoplasmic HMG protein Oxs1 acts cooperatively with Pap1 to regulate transcription. Oxs1 and Pap1 form a complex when cells are exposed to diamide or Cd that causes disulfide stress. When examined for promoters up-regulated by diamide, effective Pap1 binding to these targets requires Oxs1, and vice versa. With some genes, each protein alone enhances transcription, but the presence of both exerts an additive positive effect. In other genes, although transcription is induced by diamide, Oxs1 or Pap1 plays a negative role with full de-repression requiring loss of both proteins. In a third class of genes, Oxs1 positively regulates expression, but in its absence, Pap1 plays a negative role. The Oxs1–Pap1 regulatory interaction appears evolutionarily conserved, as heterologous (human, mouse and Arabidopsis) Oxs1 and Pap1-homologues can bind interchangeably with each other in vitro, and at least in the fission yeast, heterologous Oxs1 and Pap1-homologues can substitute for S. pombe Oxs1 and Pap1 to enhance stress tolerance.

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“…Only 4 proteins (CCDC124, IGLC6, PPIAL4D, and TRIM64B) are not classified as disease-associated according to the Open Targets Platform. In the literature, CCDC124 is mentioned in connection with cytokinesis and the associated midbody structure, a short-lived connection structure at the end of cell division [28]. IGLC6 belongs to immunoglobulins and is active in the field of immune response.…”

Section: Discussionmentioning

confidence: 99%

Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)

et al. 2021

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Objectives The aim of this investigation was the detailed analysis of the human pulp proteome using the new picosecond infrared laser (PIRL)-based sampling technique, which is based on a completely different mechanism compared to mechanical sampling. Proteome analysis of healthy pulp can provide data to define changes in the proteome associated with dental disease. Material and methods Immediately after extraction of the entire, undamaged tooth, 15 wisdom teeth were deep frozen in liquid nitrogen and preserved at −80°C. Teeth were crushed, and the excised frozen pulps were conditioned for further analysis. The pulps were sampled using PIRL, and the aspirates digested with trypsin and analyzed with mass spectrometry. Pulp proteins were categorized according to their gene ontology terminus. Proteins identified exclusively in this study were searched in the Human Protein Atlas (HPA) for gaining information about the main known localization and function. Results A total of 1348 proteins were identified in this study. The comparison with prior studies showed a match of 72%. Twenty-eight percent of the proteins were identified exclusively in this study. Considering HPA, almost half of these proteins were assigned to tissues that could be pulp specific. Conclusion PIRL is releasing proteins from the dental pulp which are not dissolved by conventional sampling techniques. Clinical Relevance The presented data extend current knowledge on dental pulp proteomics in healthy teeth and can serve as a reference for studies on pulp proteomics in dental disease.

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Coiled-Coil Domain Containing Protein 124 Is a Novel Centrosome and Midbody Protein That Interacts with the Ras-Guanine Nucleotide Exchange Factor 1B and Is Involved in Cytokinesis

Cited by 22 publications

References 51 publications

Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

A Pap1–Oxs1 signaling pathway for disulfide stress inSchizosaccharomyces pombe

Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)

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