CASEIN KINASE

Casein kinase I-depende nt phospho rylation within a PESTsequence an d u biquit ina tion a t n earby l ysines sig na l endo cytosisof yeast uracil permease. J. Biol. C he m. 275, 23608–23614.10. Zhai, L., Graves, P.R., Robinson, L.C., Italiano, M., Culbertson,M.R.,Rowles,J.,Cobb,M.H.,D[r]

termini are intracellular [5–8]. Cell surface expression ofENaC is determined by an interaction between the C tails ofb and c and the ubiquitin ligase Nedd4. The WW domainsof Nedd4 bind to the proline-rich PY motifs of b andcENaC, leading to channel ubiquitination, internalizationand degradation [9,[r]

17. Sugano, S., Andronis, C., Green, R.M., Wang, Z Y., Tobin, E.M.(1998) Protein kinase CK2 interacts with and phosphorylates theArabidopsis circadian clock-associated 1 protein. Proc. Natl Acad.Sci. US A 95, 11020–11025.18. Kalmykova, A.I., Shevelyov, Y.Y., Dobritsa, A.A., Gvozdev,V.A. (1997[r]

phosphorylation sites in Dvl-1 by replacement withacidic residues [13]. In particular, a multiple mutantwith replacement of threonines 135 and 137, as well asserines 139 and 142, by negatively charged asparticacid residues did not induce Wnt–b-catenin ⁄ Lef-1 tran-scription activation. Our phosphope[r]

viable with a double deletion of BMH1 and BMH2[16]. The strain is, however, defective in rat sar-coma ⁄ mitogen-activated protein kinase cascade signal-ling during pseudohyphal development.The mammalian 14-3-3 isoforms b and f can bephosphorylated in vivo on Ser185 [17] and, interest-ingly, S[r]

LA (2006) Analysis of a sub-proteome which co-purifieswith and is phosphorylated by the Golgi casein kinase.Cell Mol Life Sci 63, 378–389.30 Christensen B, Nielsen MS, Haselmann KF, PetersenTE & Sorensen ES (2005) Post-translationally modifiedresidues of native human osteopontin[r]

lear membrane protein family [23,24]. Such a diversearray of binding partners suggests emerin may have arole in regulating nuclear envelope structure and geneexpression. Indeed, it has been shown that cell cycletiming and Rb-MyoD myogenic transcriptional path-ways are perturbed in myoblasts isolated[r]

expressed in adult or developing testis [11], with 5–10% of genes expressed exclusively there; moreover,testis makes extensive use of alternative splicing [12]and translational control [13].Among the genes playing a role in testis function,protein kinases constitute a large group, several ofwhich ha[r]

X-100 and phosphatase inhibitors. The cleared lysatewas then subjected to immunoprecipitation using anti-body specific to SEPT2. We have previously shown[15] that immunoprecipitation of SEPT2 results in theco-immunoprecipitation of septins 6, 7 and 9 in HeLacells. As shown in Fig. 1, several phosphop[r]

mass which correlates with the mass of the peptide coveringresidues 12–27 without any modifications. In conclusion, wehave observed the peptide 12–27 in three different forms,with zero, and one and two phosphate groups attached.Peaks 41 and 43 represent peptide 12–36 with two and onephosphorylated gr[r]

activated protein kinase phosphatase-1 (MKP-1), was constitutivelyexpressed in the PC-9 cells, and its expression level was reduced byAG1478. The inhibition of JNK activation by ectopic expression ofMKP-1 or a dominant-negative form of JNK strongly suppressed AG1478-induced apoptosis. These r[r]

Fra-2 [45], FosB [46]) families. Jun and Fos proteinsdimerize via a series of leucine repeats (a leucinezipper) and bind in a sequence-specific manner to aheptad DNA sequence known as the 12-O-tetradeca-noyl-13-phorbol acetate-responsive element [47]. Theregulatory mechanism of c-fos expression by ex[r]

Together, these processes terminate the destruction ofHIF-1a. The consequence of bringing these enzymesin proximity to their substrates was illustrated in cellslacking mAKAP. Gene silencing of mAKAP bluntedhypoxia-induced HIF-1a-dependent gene transcrip-tion [28]. Delocalizing mAKAP from perinuclear[r]

This high activity is particularly striking when compared tohuman TMP kinase (kcat¼ 1s)1) [24,25].Inhibition by excess of substrate was observed for UMPand CMP but not for dCMP, AraCMP andL-3TCMP.Previous studies did not report such an inhibition, probablybecause the range of concentrations i[r]

co-receptor. Given the wealth and specificity of both kinase activity and14-3-3 binding sequences, our results suggest that the C-terminal SWTY-like motif may serve as a sensor that can selectively induce the cell surfaceexpression of membrane proteins in response to different extracellularsig[r]

UK) and incubated for one night in scintillation vials in thepresence of 1 mL of 0.1 m NaOH. The amount of radioac-tivity was determined after addition of 8 mL of scintillationliquid (Ready Protein+ Beckman). In parallel, controlmeasurements using water or BSA instead of AK1 were alsocarried out in[r]

Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1alpha. J. Biol. Chem 277, 40112–40117.52. Palmer, L.A., Gaston, B. & Johns, R.A. (2000) Normoxicstabilization of hypoxia-inducible factor-1 expression andactivity: redox-dependent effect of nitrogen oxides. Mol[r]

(a) Contributions of the various energy sources to muscle activity during mild exercise. (b) Con-sumption of glycogen stores in fast-twitch muscles during light, moderate, and heavy exercise. (c) Rate of glycogen replenishment following exhaustive exercise. (a and c adapted from Rhodes, R., andPflanz[r]

Composition per 10.0mL:Novobiocin 0.02gPreparation of Novobiocin Solution: Add novobiocin to dis-tilled/deionized water and bring volume to 10.0mL. Mix thoroughly.Filter sterilize. Preparation of Medium: Add components, except novobiocin solu-tion, to distilled/deionized water and bring volume to 99[r]