... The Author(s) 2022 This is an Accepted Manuscript; not the final Version of Record. You are encouraged to use the final Version of Record that, when published, will replace this manuscript and be freely available under a Creative Commons licence. PINK1 Phosphorylation K48-linked polyubiquitin...

... for key regulators at the protein level. However, sperm functions are known to be highly regulated by phosphorylation signaling. Here, we constructed a quantitative phosphoproteome to investigate the expression change of phosphorylated sites during sperm cryopreservation. A total of 3107 phosphorylated...

...Yanbing Wu; Haoru Wang; Chao Liu Fam20C is a Golgi kinase phosphorylating the majority of the secreted proteins. In this decade, the function of Fam20C has been largely disclosed in the loss-of function models. How the influence of the overexpressed Fam20C on cells or organs, and whether Fam20C...

... transcriptional activator and repressor activity, although how it can achieve these opposing functions remains poorly understood. We hypothesized phosphorylation status might play a role in pivoting ARX between functioning as an activator or repressor. To gain further mechanistic insight as to how ARX functions...

... studies that have revealed intricate phosphorylation-dependent mechanisms in regulating the formation and activation of the core kinase complex in the Hippo pathway. These studies have established the dimerization-mediated activation of the Hippo kinase (mammalian Ste20-like 1 and 2 (MST1/2) in mammals...

... signalling. HEY1 acts as a positive regulator of the tumour suppressor p53 via still unknown mechanisms. A MALDI-TOF/TOF MS analysis has uncovered a novel HEY1 regulatory phosphorylation event at Ser-68. Strikingly, this single phosphorylation event controls HEY1 stability and function: simulation of HEY1...

... in the de novo lipid synthesis and glycolysis pathways. The structure, turnover and transactivation potential of SREBP-1c are regulated by macronutrients and hormones via a cascade of signalling kinases. Using MS, we have identified serine 73 as a novel glycogen synthase kinase-3 (GSK-3) phosphorylation...

... ERK (extracellular-signal-regulated kinase) phosphorylates eNOS with a stoichiometry of 2–3 phosphates per eNOS monomer. Phosphorylation decreases NO synthesis and cytochrome c reductase activity. Three sites of phosphorylation were detected by MS. All sites matched the SP and TP MAPK (mitogen...

... p27 Kip1 directly. Interestingly, the lack of phosphorylation at Ser 158 of the β1 subunit promotes degradation of p27 Kip1 . We therefore propose that the β1 subunit plays a novel role in tumorigenesis by degrading p27 Kip1 . 1 Correspondence may be addressed to either of these authors (email...

... subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser 26 , a residue located within the ATP-binding site, terminates the sustained activity of the enzyme. To test the physiological importance...

...Karolina Kowalewska; Piotr Stefanowicz; Tomasz Ruman; Tomasz Frączyk; Wojciech Rode; Zbigniew Szewczuk Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological...

... subunit. Cell-cycle-stage-dependent accumulation and proteolytic degradation of different cyclin subunits regulates their association with CDKs to control different stages of cell division. CDKs promote cell cycle progression by phosphorylating critical downstream substrates to alter their activity. Here...

... previously implicated in GLUT4 trafficking. In the present study, we report that insulin stimulates the phosphorylation of Sec8 on Ser-32 in 3T3-L1 adipocytes. On the basis of the sequence around Ser-32 and the finding that phosphorylation is inhibited by the PI3K (phosphoinositide 3-kinase) inhibitor...

...Roberto Raggiaschi; Stefano Gotta; Georg C. Terstappen Protein phosphorylation is directly or indirectly involved in all important cellular events. The understanding of its regulatory role requires the discovery of the proteins involved in these processes and how, where and when protein...

... amino acid transport has not been investigated. We studied the effect the cAK-mediated phosphorylation on Na+- and Cl−-linked proline transport across the rat renal brush border membrane (BBM). cAK bioassay and Western hybridization analysis using cAK subunit-specific antibodies demonstrated...

...Dilyara A. Murtazina; Sergei P. Petukhov; Kenneth B. Storey; Alexander M. Rubtsov; Olga D. Lopina A 100-kDa protein that is a main component of the microsomal fraction from rabbit gastric mucosa is phosphorylated by cAMP-dependent protein kinase (PKA) in the presence of 0.2% Triton X-100...

... increases Ca 2+ current at any V h values. The hypothesis is put forward that, during the entrance of ground squirrels into hibernation, the phosphorylation of one of the sites (not cAMP-dependent) of L-type Ca 2+ channels is blocked. © 1999 Plenum Publishing Corporation 1999 Cardiac cells L-type...

... in distinct cell surface and intracellular forms. These two forms are glycosylated differently. In this report, we have found that (1) H-2D k antigen is phosphorylated whereas H-2K k antigen is not, and (2) only the cell surface form of H-2D k antigen is phosphorylated in thioglycolate-stimulated macrophages...

...Sung A. Lee; Ronald W. Holz; David R. Hathaway Many non-muscle cells including chromaffin cells contain actin and myosin. The 20,000 dalton light chain subunits of myosin can be phosphorylated by a Ca 2+ /calmodulin-dependent enzyme, myosin light chain kinase. In tissues other than striated muscle...

...G. Shanker; R. A. Pieringer The presence of a protein kinase capable of phosphorylating endogenous as well as exogenously added myelin basic proteins has been demonstrated in a myelin-like membrane fraction isolated from reaggregating and surface adhering, primary cultures of cells dissociated from...