The Yck2 Yeast Casein Kinase 1 Isoform Shows Cell Cycle-specific Localization to Sites of Polarized Growth and Is Required for Proper Septin Organization

Robinson, Lucy C.; Bradley, Christopher; Bryan, Joshua; Jerome, Allison; Kweon, Youngseok; Panek, Heather R.

doi:10.1091/mbc.10.4.1077

Cited by 64 publications

(77 citation statements)

References 86 publications

(122 reference statements)

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“…2C). In addition, CK1␦ has been localized to the Golgi, vesicular transporting vesicles, and plasma membrane in yeast and mammalian cells (24,(43)(44)(45)(46), consistent with the idea of CK1␦-mediated phosphorylation occurring during Cx43 connexon trafficking or after arrival at the plasma membrane. Wherever CK1 phosphorylation occurs, our cell surface biotinylation results indicate that the consequences of CK1 inhibition appear to be an accumulation of non-junctional Cx43 in the plasma membrane (Fig.…”

Section: Discussionsupporting

confidence: 56%

Casein Kinase 1 Regulates Connexin-43 Gap Junction Assembly

Cooper

Lampe

2002

Journal of Biological Chemistry

183

169

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Phosphorylation of members of the connexin family of gap junction proteins has been correlated with gap junction assembly, but the mechanisms involved remain unclear. We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.32 P i -Metabolically labeled cells treated with CKI-7, a specific CK1 inhibitor, showed a reduction in Cx43 phosphorylation on site(s) that can be phosphorylated by CK1 in vitro. To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). Immunofluorescence experiments in the presence of CK1 inhibitor showed increases in Cx43 plasma membrane localization but not necessarily accumulation at cell-cell interfaces. Decreased gap junctional and phosphorylated Cx43 was also detected when cells were treated with IC261, a CK1 inhibitor specific for ␦ or ⑀ isoforms. These data suggest CK1␦ could regulate Cx43 gap junction assembly by directly phosphorylating Cx43.

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Section: Discussionsupporting

confidence: 56%

Casein Kinase 1 Regulates Connexin-43 Gap Junction Assembly

Cooper

Lampe

2002

Journal of Biological Chemistry

183

169

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“…We previously reported that Yck2p is differentially enriched at sites of polarized secretion during the cell cycle (Robinson et al, 1999). The localization pattern we observed resembles that of proteins directed to the plasma membrane via the classical secretory pathway.…”

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confidence: 58%

Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function

Babu

Bryan

Panek

et al. 2002

Journal of Cell Science

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The S. cerevisiae Yck2 protein is a plasma membrane-associated member of the casein kinase 1 protein kinase family that, with its homolog Yck1p, is required for bud morphogenesis, cytokinesis, endocytosis and other cellular processes. Membrane localization of Yckp is critical for its function, since soluble mutants do not provide sufficient biological activity to sustain normal growth. Yck2p has neither a predicted signal sequence nor obvious transmembrane domain to achieve its plasma membrane localization, but has a C-terminal -Cys-Cys sequence that is likely to be palmitoylated. We demonstrate here that Yck2p is targeted through association with vesicular intermediates of the classical secretory pathway. Yck2p lacking C-terminal Cys residues fails to associate with any membrane, whereas substitution of these residues with a farnesyl transferase signal sequence allows sec-dependent plasma membrane targeting and biological function,suggesting that modification is required for interaction with early secretory membranes but that targeting does not require a particular modification. Deletion analysis within the 185 residue C-terminus indicates that the final 28 residues are critical for membrane association, and additional sequences just upstream are required for proper plasma membrane targeting.

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“…Actin was localized normally in Abnormal septin filaments do not contain Gin4. All bud neck proteins so far tested except for casein kinase (Robinson et al, 1999) were localized at the bud neck in a septin-dependent manner (Gladfelter et al, 2001). To examine whether the localization of a bud neck protein whose localization is dependent on septin is affected by FCF, we examined Gin4, which is a Nim1-related kinase that is localized at the bud neck in a septin-dependent manner .…”

Section: Resultsmentioning

confidence: 99%

“…Some mutations are known to cause changes in the morphology of septin filaments: ∆ gin4 , yck2 ts (Robinson et al, 1999), ∆ cla4 (Cvrckowa et al, 1995;Weiss et al, 2000), ∆ ste20 (Cvrckowa et al, 1995), ∆ bni5 (Lee et al, 2002), and elm1 (Bouquin et al, 2000) are among such mutations and they may be in factors affecting septin dynamics. Versele and Thorner (2004) showed the involvement of phosphorylation of Cdc10 by Cla4 in septin filament formation at the bud neck.…”

Section: Introductionmentioning

confidence: 99%

Forchlorfenuron, a phenylurea cytokinin, disturbs septin organization in Saccharomyces cerevisiae

et al. 2004

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Septins, which are involved in cytokinesis, have been identified in a variety of fungi and animal cells. For analysis of the function of septin, drugs targeting septin would be useful; however, no such drugs have been available hitherto. By serendipity, we found that forchlorfenuron (FCF, N-(2-chloro-4-pyridyl)-N-phenylurea, 4PU300), a synthetic plant cytokinin, disturbed cytokinesis in Saccharomyces cerevisiae . Upon administration of FCF, septin structures at the bud neck became deformed and filament-like septin appeared outside of the neck. Under these conditions, the localization of actin was normal and Gin4, which is localized at the bud neck in a septin-dependent manner, was found to remain at the location of apparently normal septin at the bud neck, whereas it was not co-localized to the deformed septin at the bud neck or to septin seen outside the bud neck. FCF administration immediately induced production of sporadic septin structures outside the bud neck, and these structures disappeared promptly upon removal of the drug. Taken together, these findings indicate that FCF maybe a promising drug for investigating the structure and function of septin.

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The Yck2 Yeast Casein Kinase 1 Isoform Shows Cell Cycle-specific Localization to Sites of Polarized Growth and Is Required for Proper Septin Organization

Cited by 64 publications

References 86 publications

Casein Kinase 1 Regulates Connexin-43 Gap Junction Assembly

Casein Kinase 1 Regulates Connexin-43 Gap Junction Assembly

Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function

Forchlorfenuron, a phenylurea cytokinin, disturbs septin organization in Saccharomyces cerevisiae

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