P-Body Localization of the Hrr25/Casein Kinase 1 Protein Kinase Is Required for the Completion of Meiosis

Zhang, Bo; Butler, Anna M.; Shi, Qian; Xing, Siyuan; Herman, Paul K.

doi:10.1128/mcb.00678-17

Cited by 11 publications

(18 citation statements)

References 66 publications

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“…CK1δ and its ortholog Hrr25 have been detected within P-bodies, cytoplasmic RNA-protein granules present in meiotic cells. This binding seems to reduce CK1 turnover into the cytoplasm, thereby preserving protein integrity for subsequent stages of meiosis (Zhang et al, 2016;Zhang et al, 2018). Localization of Hrr25 to P-bodies is necessary for completion of the meiotic program (Zhang et al, 2018).…”

Section: Ck1δ In Cell Cycle Mitosis and Meiosismentioning

confidence: 99%

“…This binding seems to reduce CK1 turnover into the cytoplasm, thereby preserving protein integrity for subsequent stages of meiosis (Zhang et al, 2016;Zhang et al, 2018). Localization of Hrr25 to P-bodies is necessary for completion of the meiotic program (Zhang et al, 2018). Hrr25 has also been observed to be involved in the induction of nuclear division of meiosis as well as in the synthesis of membranes to engulf newly synthetized nuclei, thereby mediating the exit from meiosis II (Arguello-Miranda et al, 2017).…”

Section: Ck1δ In Cell Cycle Mitosis and Meiosismentioning

confidence: 99%

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Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)

Ianes

Gärtner

et al. 2019

Gene

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Members of the highly conserved pleiotropic CK1 family of serine/threonine-specific kinases are tightly regulated in the cell and play crucial regulatory roles in multiple cellular processes from protozoa to human. Since their dysregulation as well as mutations within their coding regions contribute to the development of various different pathologies, including cancer and neurodegenerative diseases, they have become interesting new drug targets within the last decade. However, to develop optimized CK1 isoform-specific therapeutics in personalized therapy concepts, a detailed knowledge of the regulation and functions of the different CK1 isoforms, their various splice variants and orthologs is mandatory. In this review we will focus on the stressinduced CK1 isoform delta (CK1δ), thereby addressing its regulation, physiological functions, the consequences of its deregulation for the development and progression of diseases, and its potential as therapeutic drug target.

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Section: Ck1δ In Cell Cycle Mitosis and Meiosismentioning

confidence: 99%

Section: Ck1δ In Cell Cycle Mitosis and Meiosismentioning

confidence: 99%

Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)

Ianes

Gärtner

et al. 2019

Gene

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“…Yck3 is a vacuolar membrane-localized kinase that mediates vacuolar membrane fusion (LAGRASSA AND UNGERMANN 2005; ZICK AND WICKNER 2012;LAWRENCE et al 2014). Hrr25 is implicated in multiple cellular processes, including vesicular trafficking, ribosome biogenesis, autophagy, transcriptional regulation, meiosis, endocytosis, microtubule assembly and spindle positioning, and DNA damage response (HOEKSTRA et al 1991;PETRONCZKI et al 2006;SCHAFER et al 2006;RAY et al 2008;MEHLGARTEN et al 2009; CORBETT AND HARRISON 2012;SARKAR et al 2013;MOCHIDA et al 2014;PFAFFENWIMMER et al 2014;TANAKA et al 2014;ABDEL-FATTAH et al 2015;GHALEI et al 2015;NAKATOGAWA 2015;PENG et al 2015a;PENG et al 2015b;DAVIS et al 2016;ARGUELLO-MIRANDA et al 2017;COLLINS et al 2017;ZHANG et al 2018;ZIENTARA-RYTTER et al 2018;NEMEC et al 2019). The kinase domains of these four casein kinase I isoforms are highly similar, while the sequences outside the kinase domain are not conserved (WANG et al 1996;GROSS AND ANDERSON 1998).…”

Section: Introductionmentioning

confidence: 99%

“…Consistent with its multiple cellular functions, Hrr25 is localized to different cellular locations, including endocytic sites, bud neck, P-bodies, spindle pole bodies, and the nucleus (PENG et al 2015a;PENG et al 2015b;ZHANG et al 2016). Hrr25 has an N-terminal kinase domain, a middle region, and a C-terminal P/Q rich region (DHILLON AND HOEKSTRA 1994;PENG et al 2015a;PENG et al 2015b;YE et al 2016;ZHANG et al 2016;ZHANG et al 2018). The middle region has been proposed or shown to be required for Hrr25's localization to P-bodies, spindle pole bodies, endocytic sites, and meiosis I centromeres.…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial Biogenesis Is Positively Regulated by Casein Kinase I Hrr25 Through Phosphorylation of Puf3 in Saccharomyces cerevisiae

Bhondeley¹,

Liu

2020

Genetics

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Mitochondrial biogenesis requires coordinated expression of genes encoding mitochondrial proteins, which in Saccharomyces cerevisiae is achieved in part via post-transcriptional control by the Pumilio RNA-binding domain protein Puf3. Puf3 binds to the 3′-UTR of many messenger RNAs (mRNAs) that encode mitochondrial proteins, regulating their turnover, translation, and/or mitochondrial targeting. Puf3 hyperphosphorylation correlates with increased mitochondrial biogenesis; however, the kinase responsible for Puf3 phosphorylation is unclear. Here, we show that the casein kinase I protein Hrr25 negatively regulates Puf3 by mediating its phosphorylation. An hrr25 mutation results in reduced phosphorylation of Puf3in vivo and a puf3 deletion mutation reverses growth defects of hrr25 mutant cells grown on medium with a nonfermentable carbon source. We show that Hrr25 directly phosphorylates Puf3, and that the interaction between Puf3 and Hrr25 is mediated through the N-terminal domain of Puf3 and the kinase domain of Hrr25. We further found that an hrr25 mutation reduces GFP expression from GFP reporter constructs carrying the 3′-UTR of Puf3 targets. Downregulation of GFP expression due to an hrr25 mutation can be reversed either by puf3Δ or by mutations to the Puf3-binding sites in the 3′-UTR of the GFP reporter constructs. Together, our data indicate that Hrr25 is a positive regulator of mitochondrial biogenesis by phosphorylating Puf3 and inhibiting its function in downregulating target mRNAs encoding mitochondrial proteins.

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“…For example, the presence in SGs of regulators of a stress-responsive MAPK pathway determines whether cells undergo apoptosis in response to certain stresses (Arimoto et al 2008). In addition, the recruitment of the budding yeast CK1 protein kinase Hrr25 to the P-body has been shown to be important for the efficient completion of meiosis (Zhang et al 2018). As a result of these types of studies, it has been suggested that these RNP granules might play a role in the reprograming of specific signaling networks in response to stress (Kedersha et al 2013;Shah et al 2014).…”

mentioning

confidence: 99%

Insights into the Role of P-Bodies and Stress Granules in Protein Quality Control

Nostramo¹,

Xing²,

Zhang³

et al. 2019

Genetics

Self Cite

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The eukaryotic cell is highly compartmentalized, and contains a variety of both membrane-bound and membraneless organelles. The latter include the cytoplasmic ribonucleoprotein (RNP) granules, known as the processing body (P-body) and the stress granule. These RNP structures are thought to be involved in the storage of particular mRNAs during periods of stress. Here, we find that a mutant lacking both P-bodies and stress granules exhibits phenotypes suggesting that these structures also have a role in the maintenance of protein homeostasis. In particular, there was an increased occurrence of specific protein quality control (PQC) compartments in this mutant, an observation that is consistent with there being an elevated level of protein misfolding. These compartments normally house soluble misfolded proteins and allow the cell to sequester these polypeptides away from the remaining cellular milieu. Moreover, specific proteins that are normally targeted to both P-bodies and stress granules were found to instead associate with these PQC compartments in this granuleless mutant. This observation is interesting as our data indicate that this association occurs specifically in cells that have been subjected to an elevated level of proteotoxic stress. Altogether, the results here are consistent with P-bodies and stress granules having a role in normal protein homeostasis in eukaryotic cells. KEYWORDS processing bodies; stress granules; protein quality control compartments; protein homeostasis T HE eukaryotic cell is segregated into distinct functional domains by the presence of a variety of both membranebound and membraneless organelles. The former have been extensively studied and include structures like the mitochondria, nucleus, and endoplasmic reticulum. The latter differ fundamentally from these well-characterized compartments in that they lack a limiting membrane (Hyman et al. 2014). However, it is likely that they serve similar purposes in the cell. For example, macromolecules participating in a related process can be concentrated in these structures so as to increase reaction efficiencies (Jin et al. 2017). Although several of these membraneless compartments, like the nucleolus and centrosome, have been studied for decades, most have been identified more recently. Many of these structures have been found to exhibit liquid-like properties in the cell and to assemble (and disassemble) rapidly in response to specific environmental signals (

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P-Body Localization of the Hrr25/Casein Kinase 1 Protein Kinase Is Required for the Completion of Meiosis

Cited by 11 publications

References 66 publications

Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)

Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)

Mitochondrial Biogenesis Is Positively Regulated by Casein Kinase I Hrr25 Through Phosphorylation of Puf3 in Saccharomyces cerevisiae

Insights into the Role of P-Bodies and Stress Granules in Protein Quality Control

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