Cytoplasmic forms of fission yeast casein kinase-1 associate primarily with the particulate fraction of the cell.

Wang, Pichao; Vančura, Aleš; Desai, Aparna; Carmel, Gilles; Kuret, Jeff

doi:10.1016/s0021-9258(17)32675-3

Cited by 35 publications

(1 citation statement)

References 46 publications

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“…CK1α regulation is primarily involved in the transport, sub-cellular localization, activation/inactivation, and degradation of substrates [ 32 ]. CK1α can localize to the nucleus, where it regulates mRNA metabolism [ 33 ]. Furthermore, GLIPR1 mediates CK1α redistribution from the Golgi to the cytoplasm and increases CK1 protein levels, which are crucial to the phosphorylation and destruction of β-catenin [ 34 ].…”

Section: Discussionmentioning

confidence: 99%

Casein Kinase 1α as a Novel Factor Affects Thyrotropin Synthesis via PKC/ERK/CREB Signaling

Wang

Zhang

et al. 2023

IJMS

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Casein kinase 1α (CK1α) is present in multiple cellular organelles and plays various roles in regulating neuroendocrine metabolism. Herein, we investigated the underlying function and mechanisms of CK1α-regulated thyrotropin (thyroid-stimulating hormone (TSH)) synthesis in a murine model. Immunohistochemistry and immunofluorescence staining were performed to detect CK1α expression in murine pituitary tissue and its localization to specific cell types. Tshb mRNA expression in anterior pituitary was detected using real-time and radioimmunoassay techniques after CK1α activity was promoted and inhibited in vivo and in vitro. Relationships among TRH/L-T4, CK1α, and TSH were analyzed with TRH and L-T4 treatment, as well as thyroidectomy, in vivo. In mice, CK1α was expressed at higher levels in the pituitary gland tissue than in the thyroid, adrenal gland, or liver. However, inhibiting endogenous CK1α activity in the anterior pituitary and primary pituitary cells significantly increased TSH expression and attenuated the inhibitory effect of L-T4 on TSH. In contrast, CK1α activation weakened TSH stimulation by thyrotropin-releasing hormone (TRH) by suppressing protein kinase C (PKC)/extracellular signal-regulated kinase (ERK)/cAMP response element binding (CREB) signaling. CK1α, as a negative regulator, mediates TRH and L-T4 upstream signaling by targeting PKC, thus affecting TSH expression and downregulating ERK1/2 phosphorylation and CREB transcriptional activity.

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Section: Discussionmentioning

confidence: 99%

Casein Kinase 1α as a Novel Factor Affects Thyrotropin Synthesis via PKC/ERK/CREB Signaling

Wang

Zhang

et al. 2023

IJMS

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Casein kinases

Pyerin¹,

and²,

Lorenz³

1996

Protein Phosphorylation

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Characterization of two protein kinases from Schizosaccharomyces pombe involved in the regulation of DNA repair.

1994

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We have identified two novel genes designated hhp1+ and hhp2+ in the fission yeast Schizosaccharomyces pombe. The hhp1+ and hhp2+ genes encode two closely related protein kinases that share significant sequence identities with Hrr25p from Saccharomyces cerevisiae. Characterization of strains harboring single and double mutations in the hhp+ genes reveals DNA repair defects in these cells. Schizosaccharomyces pombe strains lacking either or both Hhp activities reveal differences in their ability to withstand DNA lesions caused by either methyl methanesulfonate (MMS) or gamma‐rays which correlate with their ability to repair DNA strand breaks caused by these agents. We suggest that Hhp1 and Hhp2 are involved in the regulation of distinct and overlapping DNA repair pathways in S. pombe.

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Cytoplasmic forms of fission yeast casein kinase-1 associate primarily with the particulate fraction of the cell.

Cited by 35 publications

References 46 publications

Casein Kinase 1α as a Novel Factor Affects Thyrotropin Synthesis via PKC/ERK/CREB Signaling

Casein Kinase 1α as a Novel Factor Affects Thyrotropin Synthesis via PKC/ERK/CREB Signaling

Casein kinases

Characterization of two protein kinases from Schizosaccharomyces pombe involved in the regulation of DNA repair.

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