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Posttranslational Modifications and Protein Function

Year 2012, Volume: 31 Issue: 1, 29 - 38, 01.06.2012

Abstract

Many proteins undergo a process called posttranslational modification (PTM) in order to acquire functional capabilities. PTM of proteins provide prokaryotic and eukaryotic cells with highly versatile tools and tricks, which can be used in the spatial and temporal regulation of key proteins and variety of cellular processes controlled by proteins. The number and types of posttranslational modifications (PTMs) that a protein can accommodate at any given time can be staggering. The major types of PTMs frequently observed and well-studied
in eukaryotic cells include phosphorylation, glycosylation, acetylation, acylation, prenylation, methylation, ubiquitylation, and proteolytic cleavage. Enzymes dedicated to protein modifications are in the orders of thousands. An understanding of types and levels of PTMs of proteins and enzymes dedicated to this process should provide us with better opportunities to study protein function and diseases associated with aberrant modification of proteins.

References

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  • for posttranslational
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Posttranslasyonel Modifikasyon ve Protein Fonksiyonu

Year 2012, Volume: 31 Issue: 1, 29 - 38, 01.06.2012

Abstract

Birçok protein fonksiyon gösterebilmesi için posttranslasyonel modifikasyon (PTM) adı verilen bir işleme tabi tutulur. PTM, proteinlerin yersel ve zamansal regülasyonunda ve proteinler tarafından gerçekleştirilen önemli hücresel faaliyetlerin kontrolünde ökaryotik ve prokaryotik hücreler tarafından kullanılan önemli bir araçtır. Herhangi bir zamanda herhangi bir proteinin maruz kaldığı PTM sayısı ve tipi çok fazla olabilir. Ökaryotik hücrelerde sık karşılaşılan ve nispeten detaylı olarak çalışılmış PTM tipleri olarak fosforilasyon, glikozilasyon, asetilasyon, açilasyon, prenilasyon, metilasyon, ubiqutilasyon ve proteolitik parçalanma sayılabilir. Bu tip PTM`ları gerçekleştiren enzimlerin sayısı binleri bulmaktadır. PTM ve bu işlemde görevli enzimlerin iyi kavranması ve çalışılması bize, protein foksiyonu ve hastalıklarla ilişkili anormal PTM`ların anlaşılması için daha iyi fırsatlar sunacaktır

References

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  • Arozarena, I., Calvo, F., Crespo, P., 2011. Ras, an actor on many stages: posttranslational modifications, localization, and site-specified events. Genes Cancer 2, 182-194.
  • Bai, G., Zhang, Z.J., Werner, R., Nuttal, F.Q., Tan, A.W., Lee, E.Y., 1990. The primary structure of rat liver glycogen synthase deduced by cDNA cloning. Absence of phosphorylation sites 1a and 1b. J Biol Chem 265, 7843-7848.
  • Basso, A.D., Kirschmeier, P., Bishop, W.R., 2006. Lipid posttranslational modifications. Farnesyl transferase inhibitors. J Lipid Res 47, 15-31.
  • Bauzon, F., Zhu, L., 2010. Racing to block tumorigenesis after pRb loss: an innocuous point mutation wins with synthetic lethality. Cell Cycle 9, 2118-2123.
  • Blom, N., Sicheritz-Ponten, T., Gupta, R., Gammeltoft, S., Brunak, S., 2004. Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649.
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  • Burlingame, A.L., Zhang, X., Chalkley, R.J., 2005. Mass spectrometric analysis of histone posttranslational modifications. Methods 36, 383- 394.
  • Carpenter, G.H., Proctor, G.B., 1999. O-linked glycosylation occurs on basic parotid salivary proline-rich proteins. Oral Microbiol Immunol 14, 309-315.
  • Case, N., Thomas, J., Sen, B., Styner, M., Xie, Z., Galibor, K., Rubin, J., 2011. Mechanical regulation of glycogen synthase kinase 3beta (GSK3beta) in mesenchymal stem cells is dependent on Akt protein serine 473 phosphorylation via mTORC2 protein. J Biol Chem 286, 39450-39456.
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  • Diehl, J.A., Cheng, M., Roussel, M.F., Sherr, C.J., 1998. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 12, 3499-3511.
  • Dolence, J.M., Poulter, C.D., 1995. A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Proc Natl Acad Sci U S A 92, 5008-5011.
  • Eastman, R.T., Buckner, F.S., Yokoyama, K., Gelb, M.H., Van Voorhis, W.C., 2006. Thematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylation. J Lipid Res 47, 233-240.
  • Eisenhaber, B., Eisenhaber, F., 2007. Posttranslational modifications and subcellular localization signals: indicators of sequence regions without inherent 3D structure? Curr Protein Pept Sci 8, 197-203.
  • Eisenhaber, F., Eisenhaber, B., Kubina, W., Maurer-Stroh, S., Neuberger, G., Schneider, G., Wildpaner, M., 2003. Prediction of lipid posttranslational modifications and localization signals from protein sequences: big-Pi, NMT and PTS1. Nucleic Acids Res 31, 3631-3634.
  • Freitas, M., Axelsson, L.G., Cayuela, C., Midtvedt, T., Trugnan, G., 2005. Indigenous microbes and their soluble factors differentially modulate intestinal glycosylation steps in vivo. Use of a "lectin assay" to survey in vivo glycosylation changes. Histochem Cell Biol 124, 423-433.
  • Fuchs, O., Neuwirtova, R., 2006. [Ubiquitins, proteasomes, sumoylation and application today and in future for cancer and other diseases therapy II. Sumoylation and neddylation as posttranslational modifications of proteins and their ubiquitinylation and its significance]. Vnitr Lek 52, 619-627.
  • Funayama, R., Ishikawa, F., 2007. Cellular senescence and chromatin structure. Chromosoma 116, 431-440.
  • Garina, D.V., Kuz'mina, V.V., Gerasimov, Y.V., 2007. The effect of epinephrine on feeding and motion patterns in goldfish Carassius auratus (L.). Comp Biochem Physiol A Mol Integr Physiol 148, 544-549.
  • Germain, D., Russell, A., Thompson, A., Hendley, J., 2000. Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286. J Biol Chem 275, 12074-12079.
  • Hale, B.G., Knebel, A., Botting, C.H., Galloway, C.S., Precious, B.L., Jackson, D., Elliot, R.M., Randall, R.E., 2009. CDK/ERK-mediated phosphorylation of the human influenza A virus NS1 protein at threonine-215. Virology 383, 6- 11.
  • Hallenbeck, P.C., Walsh, D.A., 1986. Control of phosphorylase kinase in the isolated glycogen particle by Ca2+-Mg2+ synergistic activation and cAMP-dependent phosphorylation. J Biol Chem 261, 5442-5449.
  • Lau, P.P., Van Handel, M., Larvin, M., McMahon, M.J., Geokas, M.C., 1990. Proteolytic degradation of human recombinant proinsu- lin/insulin by sera from acute pancreatitis patients and complete inhibition by Eglin-C. Pancreas 5, 17-26.
  • Lodish, H., Zipursky, S.L., Matsudaira, P., Baltimore, D., Darnell, J., 2000. Molecular Cell Biology. New York: W. H. Freeman
  • Israel, M., Schwartz, L., 2011. The metabolic advantage of tumor cells. Mol Cancer 10, 70.
  • Issad, T., Masson, E., Pagesy, P., 2010. O- GlcNAc modification, insulin signaling and diabetic complications. Diabetes Metab 36, 423- 435.
  • Jacob, T., Van den Broeke, C., Favoreel, H.W., 2011. Viral serine/threonine protein kinases. J Virol 85, 1158-1173.
  • Jensen, J., Gronning-Wang, L.M., Jebens, E., Whitehead, J.B., Zorec, R., Shepherd, P.R., 2008. Adrenaline potentiates insulin-stimulated PKB activation in the rat fast-twitch epitrochlearis muscle without affecting IRS-1-associated PI 3- kinase activity. Pflugers Arch 456, 969-978.
  • Jensen, J., Ruge, T., Lai, Y.C., Svensson, M.K., Eriksson, J.W., 2011. Effects of adrenaline on whole-body glucose metabolism and insulin- mediated regulation of glycogen synthase and PKB phosphorylation in human skeletal muscle. Metabolism 60, 215-226.
  • Jiang, S., Fang, Q., Zhang, F., Weisz, O.A., 2011. Functional characterization of insulin receptor gene mutations contributing to Rabson- Mendenhall syndrome - phenotypic heterogeneity of insulin receptor gene mutations. Endocr J 58, 931-940.
  • Johnson, L.N. 1992. Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J 6, 2274-2282.
  • Johnson, L.N., Hu, S.H., Barford, D., 1992. Catalytic mechanism of glycogen phosphorylase. Faraday Discuss, 131-142.
  • Kikuchi, K., Yamada, T., Sugi, H., 2009. Effects of adrenaline on glycogenolysis in resting anaerobic frog muscles studied by 31P-NMR. J Physiol Sci 59, 439-446.
  • Ko, H.S., Lee, Y., Shin, J.H., Karuppagounder, S. S., Gadag, B.S., Koleske, A.J., Pletnikova, O., Troncoso, J.C., Dawson, V.L., Dawson, T.M., 2010. Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proc Natl Acad Sci U S A 107, 16691-16696.
  • Krueger, K.E., Srivastava, S., 2006. Posttranslational protein modifications: current implications for cancer detection, prevention, and therapeutics. Mol Cell Proteomics 5, 1799-1810.
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Primary Language Turkish
Journal Section Articles
Authors

Abdullah Yalçın This is me

Publication Date June 1, 2012
Published in Issue Year 2012 Volume: 31 Issue: 1

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APA Yalçın, A. (2012). Posttranslasyonel Modifikasyon ve Protein Fonksiyonu. Uludağ Üniversitesi Veteriner Fakültesi Dergisi, 31(1), 29-38.
AMA Yalçın A. Posttranslasyonel Modifikasyon ve Protein Fonksiyonu. Uludağ Üniversitesi Veteriner Fakültesi Dergisi. June 2012;31(1):29-38.
Chicago Yalçın, Abdullah. “Posttranslasyonel Modifikasyon Ve Protein Fonksiyonu”. Uludağ Üniversitesi Veteriner Fakültesi Dergisi 31, no. 1 (June 2012): 29-38.
EndNote Yalçın A (June 1, 2012) Posttranslasyonel Modifikasyon ve Protein Fonksiyonu. Uludağ Üniversitesi Veteriner Fakültesi Dergisi 31 1 29–38.
IEEE A. Yalçın, “Posttranslasyonel Modifikasyon ve Protein Fonksiyonu”, Uludağ Üniversitesi Veteriner Fakültesi Dergisi, vol. 31, no. 1, pp. 29–38, 2012.
ISNAD Yalçın, Abdullah. “Posttranslasyonel Modifikasyon Ve Protein Fonksiyonu”. Uludağ Üniversitesi Veteriner Fakültesi Dergisi 31/1 (June 2012), 29-38.
JAMA Yalçın A. Posttranslasyonel Modifikasyon ve Protein Fonksiyonu. Uludağ Üniversitesi Veteriner Fakültesi Dergisi. 2012;31:29–38.
MLA Yalçın, Abdullah. “Posttranslasyonel Modifikasyon Ve Protein Fonksiyonu”. Uludağ Üniversitesi Veteriner Fakültesi Dergisi, vol. 31, no. 1, 2012, pp. 29-38.
Vancouver Yalçın A. Posttranslasyonel Modifikasyon ve Protein Fonksiyonu. Uludağ Üniversitesi Veteriner Fakültesi Dergisi. 2012;31(1):29-38.