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Literature summary for 2.7.11.1 extracted from
- The casein kinases Yck1p and Yck2p act in the secretory pathway, in part, by regulating the Rab exchange factor Sec2p (2016), Mol. Biol. Cell, 27, 686-701 .
No PubMed abstract available
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | D-glucose promotes Sec2p phosphorylation | Saccharomyces cerevisiae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli | Saccharomyces cerevisiae |
| recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli, overexpression of GFP-tagged Yck2p wild-type and mutant enzymes in Saccharomyces cerevisiae | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H187Y | a dead kinase allele, inactive Yck2p mutant | Saccharomyces cerevisiae |
| additional information | construction of a Yck1pDELTA enzyme knockout strain | Saccharomyces cerevisiae |
| additional information | construction of a Yck2pDELTA enzyme knockout strain | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Sec2p phosphorylation is affected in Pik1p and Sac1p mutants | Saccharomyces cerevisiae | |
| phosphatidylinositol-4-phosphate | inhibits Sec2p phosphorylation by Yck2p | Saccharomyces cerevisiae |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plasma membrane | - |
Saccharomyces cerevisiae | 5886 | - |
| secretory vesicle | - |
Saccharomyces cerevisiae | 99503 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + Sec2p | Saccharomyces cerevisiae | - |
ADP + phospho-Sec2p | - |
? | |
| ATP + Sec2p | Saccharomyces cerevisiae BY4741 | - |
ADP + phospho-Sec2p | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
and diverse modified strains, overview | - |
| Saccharomyces cerevisiae BY4741 | - |
and diverse modified strains, overview | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| lipoprotein | Yck1p and Yck2p are lipid-modified kinases that ride on secretory vesicles to reach the plasma membrane | Saccharomyces cerevisiae |
| phosphoprotein | the Yck2p protein appears to undergo autophosphorylation after addition of ATP | Saccharomyces cerevisiae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + Sec2p | - |
Saccharomyces cerevisiae | ADP + phospho-Sec2p | - |
? | |
| ATP + Sec2p | wild-type Sec2p and recombinant GST-tagged Sec2p 1-508 protein | Saccharomyces cerevisiae | ADP + phospho-Sec2p | - |
? | |
| ATP + Sec2p | - |
Saccharomyces cerevisiae BY4741 | ADP + phospho-Sec2p | - |
? | |
| ATP + Sec2p | wild-type Sec2p and recombinant GST-tagged Sec2p 1-508 protein | Saccharomyces cerevisiae BY4741 | ADP + phospho-Sec2p | - |
? | |
| additional information | Yck2p protein performs autophosphorylation. The casein kinase Yck2p binds to the autoinhibitory region of Sec2p and phosphorylates Sec2p in vitro and in vivo, phosphorylation of the phosphoregion at amino acids 181-188 | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | Yck2p protein performs autophosphorylation. The casein kinase Yck2p binds to the autoinhibitory region of Sec2p and phosphorylates Sec2p in vitro and in vivo, phosphorylation of the phosphoregion at amino acids 181-188 | Saccharomyces cerevisiae BY4741 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| casein kinase | - |
Saccharomyces cerevisiae |
| Yck1p | - |
Saccharomyces cerevisiae |
| Yck2p | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Saccharomyces cerevisiae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | loss of Yck1p and Yck2p function leads to accumulation of an intracellular pool of the secreted glucanase Bgl2p, as well as to accumulation of Golgi-related structures in the cytoplasm. The Rab GTPase Sec2p is only partially phosphorylated in yck1DELTA and yck2DELTA mutants | Saccharomyces cerevisiae |
| malfunction | loss of Yck1p and Yck2p function leads to accumulation of an intracellular pool of the secreted glucanase Bgl2p, as well as to accumulation of Golgi-related structures in the cytoplasm. The Rab GTPase Sec2p is only partially phosphorylated in yck1DELTA and yck2DELTA mutants. Sec2p localization is modestly affected in a sensitized background when YCK2 is deleted | Saccharomyces cerevisiae |
| metabolism | Sec2p is a guanine nucleotide exchange factor that activates Sec4p, the final Rab GTPase of the yeast secretory pathway. Sec2p is recruited to secretory vesicles by the upstream Rab Ypt32p acting in concert with phosphatidylinositol-4-phosphate. Sec2p also binds to the Sec4p effector Sec15p, yet Ypt32p and Sec15p compete against each other for binding to Sec2p. the region of aa 450508, named the autoinhibitory region, negatively regulates Sec15p binding to Sec2p by an autoinhibitory mechanism . The redundant casein kinases Yck1p and Yck2p phosphorylate sites within the Ypt32p/Sec15p binding region and in doing so promote binding to Sec15p and inhibit binding to Ypt32p. Sec2p is phosphorylated after it is recruited to secretory vesicles and the level of phosphatidylinositol-4-phosphate is reduced. This promotes Sec2p function by stimulating its interaction with Sec15p. Finally, Sec2p is dephosphorylated very late in the exocytic reaction to facilitate recycling. Metabolic regulatory network overview. the kinases Yck1/2p play an active role at one or more stages of the secretory pathway | Saccharomyces cerevisiae |
| metabolism | Sec2p is a guanine nucleotide exchange factor that activates Sec4p, the final Rab GTPase of the yeast secretory pathway. Sec2p is recruited to secretory vesicles by the upstream Rab Ypt32p acting in concert with phosphatidylinositol-4-phosphate. Sec2p also binds to the Sec4p effector Sec15p, yet Ypt32p and Sec15p compete against each other for binding to Sec2p. the region of aa 450508, named the autoinhibitory region, negatively regulates Sec15p binding to Sec2p by an autoinhibitory mechanism. The redundant casein kinases Yck1p and Yck2p phosphorylate sites within the Ypt32p/Sec15p binding region and in doing so promote binding to Sec15p and inhibit binding to Ypt32p. Sec2p is phosphorylated after it is recruited to secretory vesicles and the level of phosphatidylinositol-4-phosphate is reduced. This promotes Sec2p function by stimulating its interaction with Sec15p. Finally, Sec2p is dephosphorylated very late in the exocytic reaction to facilitate recycling. Metabolic regulatory network overview. The kinases Yck1/2p play an active role at one or more stages of the secretory pathway | Saccharomyces cerevisiae |
| physiological function | casein kinases Yck1p and Yck2p act in the secretory pathway, in part, by regulating the Rab exchange factor Sec2p. The redundant casein kinases Yck1p and Yck2p phosphorylate sites within the Ypt32p/Sec15p binding region and in doing so promote binding to Sec15p and inhibit binding to Ypt32p. Sec2p phosphorylation is important to ensure efficient vesicular transport and Yck1p and Yck2p are important for secretion. But Yck1p and Yck2p have additional target(s) other than Sec2p, which act upstream on the secretory pathway | Saccharomyces cerevisiae |
| physiological function | casein kinases Yck1p and Yck2p act in the secretory pathway, in part, by regulating the Rab exchange factor Sec2p. The redundant casein kinases Yck1p and Yck2p phosphorylate sites within the Ypt32p/Sec15p binding region and in doing so promote binding to Sec15p and inhibit binding to Ypt32p. Yck2p binds to the autoinhibitory domain of Sec2p, adjacent to the phosphatidylinositol-4-phosphate binding site, and addition of phosphatidylinositol-4-phosphate inhibits Sec2p phosphorylation by Yck2p. Sec2p phosphorylation is important to ensure efficient vesicular transport and Yck1p and Yck2p are important for secretion. But Yck1p and Yck2p have additional target(s) other than Sec2p, which act upstream on the secretory pathway. Genetic interactions between yck2 and components of the secretory machinery, overview | Saccharomyces cerevisiae |
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