Abstract
Mitochondria contain their own DNA, they divide throughout interphase and are distributed randomly between daughter cells during cell division. Most mitochondrial proteins are encoded in the nucleus and produced in the cytosol. They are then imported into the mitochondria via the TOM/TIM transport system, which recognises them by a specific localisation sequence which is cleaved off once a protein has entered a mitochondrium. Mitochondrial lipids are made by the ER. Similar pathways exist for plastids, peroxisomes and nucleus. However, nuclear transport sequences are not removed after transport as the nuclear membrane breaks down during mitosis, releasing nuclear proteins into the cytosol. They need to be reimported afterwards. Insertion of proteins into the ER occurs cotranslationally. While they are transported into the ER, proteins are glycosylated. The oligosaccharides added to Thr or Ser or Hyl (O-linked) are simple, but some are important as blood group antigens. Very complex sugar trees are added to Asn (N-linked). These trees play an important role in the quality control of the ER, which prevents the production of misfolded proteins. Additional sugar residues are added during the protein’s passage through the Golgi apparatus.
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References
M. Aebi, N-linked protein glycosylation in the ER. Biochim. Biophys. Acta 1833(11), 2430–2437 (2013). doi: 10.1016/j.bbamcr.2013.04.001
T. Ast, G. Cohen, M. Schuldiner, A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum. Cell 152(5), 1134–1145 (2013). doi: 10.1016/j.cell.2013.02.003
J.J. Barrott, T.A.J. Haystead, Hsp90, an unlikely ally in the war on cancer. FEBS J. 280(6), 1381–1396 (2013). doi: 10.1111/febs.12147
J.A. Boelens, S. Lust, F. Offner, M.E. Bracke, B.W. Vanhoecke, The endoplasmic reticulum: A target for new anticancer drugs. In Vivo 21(2), 215–226 (2007). URL http://iv.iiarjournals.org/content/21/2/215.full.pdf+html
E. Buxbaum, Biophysical Chemistry of Proteins: An Introduction to Laboratory Methods (Springer, New York, 2011). ISBN 978-1-4419-7250-7
C.M. Cabral, Y. Liu, R.N. Sifers, Dissecting glycoprotein quality control in the secretory pathway. Trends Bichem. Sci. 26, 619–624 (2001). doi: 10.1016/S0968-0004(01)01942-9
D. Calo, L. Kaminski, J. Eichler, Protein glycosylation in archaea: Sweet and extreme. Glycobiology 20(9), 1065–1076 (2010). doi: 10.1093/glycob/cwq055
B. Cylwik, K. Lipartowska, L. Chrostek, E. Gruszewska, Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation. Acta Biochim. Pol. 60(2), 151–161 (2013a). URL http://www.actabp.pl/pdf/3_2013/361.pdf
B. Cylwik, K. Lipartowska, L. Chrostek, E. Gruszewska, Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation. Acta Biochim. Pol. 60(3), 361–368 (2013b). URL http://www.actabp.pl/pdf/3_2013/361.pdf
T. de Beer, J.F.G. Vliegenthart, A.S. Loeffler, J. Hofsteenge, The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase us is α-mannopyranose. Biochemistry 34(37), 11785–11789 (1995). doi: 10.1021/bi00037a016
A. Dell, A. Galadari, F. Sastre, P. Hitchen, Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes. Int. J. Microbiol. 2010, Article ID 148178 (2010). doi: 10.1155/2010/148178
V. Denic, A portrait of the GET pathway as a surprisingly complicated young man. Trends Biochem. Sci. 37(10), 411–417 (2012). doi: 10.1016/j.tibs.2012.07.004
J. Dudley, H. Byun, Y. Gou, A. Zook, M. Lozano, ERAD and how viruses exploit it. Frontiers Microbiol. 5, Art. No. 330 (2014). doi: 10.3389/fmicb.2014.00330
T. Endo, K. Yamano, Transport of proteins across or into the mitochondrial outer membrane. Biochim. Biophys. Acta 1803(6), 706–714 (2010). doi: 10.1016/j.bbamcr.2009.11.007
S.P. Ferris, V.K. Kodali, R.J. Kaufman, Glycoprotein folding and quality-control mechanisms in protein-folding diseases. Dis. Models Mech. 7(3), 331–341 (2014). doi: 10.1242/dmm.014589
K.S. George, S. Wu, Lipid raft: A floating island of death or survival. Toxicol. Appl. Pharmacol. 259(3), 311–319 (2012). doi: 10.1016/j.taap.2012.01.007
Y. Ishibashi, A. Kohyama-Koganeya, Y. Hirabayashi, New insights on glucosylated lipids: Metabolism and functions. Biochim. Biophys. Acta 1831(9), 1475–1485 (2013). doi: 10.1016/j.bbalip.2013.06.001
E. Klotzsch, G.J. SchĂĽtz, A critical survey of methods to detect plasma membrane rafts. Phil. Trans. Roy. Soc. Lond. B: Biol. Sci. 368(1611), (2012). doi: 10.1098/rstb.2012.0033
B. Franz Lang, Mitochondria and the origin of eukaryotes, in ed.by W. Löffelhardt, Endosymbiosis (Springer, Vienna, 2014), pp. 3–18. ISBN 978-3-7091-1302-8. doi: 10.1007/978-3-7091-1303-5_1
M. Mehnert, T. Sommer, E. Jarosch, ERAD ubiquitin ligases. BioEssays 32(10), 905–913 (2010). doi: 10.1002/bies.201000046
P.G. Needham, J.L. Brodsky, How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochim. Biophys. Acta 1833(11), 2447–2457 (2013). doi: 10.1016/j.bbamcr.2013.03.018
H. Nothaft, C.M. Szymanski, Bacterial protein N-glycosylation: New perspectives and applications. J. Biol. Chem. 288(10), 6912–6920 (2013). doi: 10.1074/jbc.R112.417857
D.M. Owen, K. Gaus, Imaging lipid domains in cell membranes: the advent of super-resolution fluorescence microscopy. Front. Plant Sci. 4(503), (2013). doi: 10.3389/fpls.2013.00503
A.J. Parodi, Protein glycosylation and its role in protein folding. Annu. Rev. Biochem. 69, 69–93 (2000). doi: 10.1146/annurev.biochem.69.1.69
A. Ruggiano, O. Foresti, P. Carvalho, ER-associated degradation: Protein quality control and beyond. J. Cell Biol. 204(6), 869–879 (2014). doi: 10.1083/jcb.201312042
B. Schiller, A. Hykollari, S. Yan, K. Paschinger, I.B.H. Wilson, Complicated N-linked glycans in simple organisms. Biol. Chem. 393(8), 661–673 (2012). doi: 10.1515/hsz-2012-0150
A. Shah, D. Chen, A.R. Boda, L.J. Foster, M.J. Davis, M.M. Hill, Raftprot: mammalian lipid raft proteome database. Nucleic Acids Res. (2014). doi: 10.1093/nar/gku1131
S. Shao, R.S. Hegde, Membrane protein insertion at the endoplasmic reticulum. Annu. Rev. Cell. Dev. Biol. 27(1), 25–56 (2011). doi: 10.1146/annurev-cellbio-092910-154125
K. Simons, E. Ikonen, Functional rafts in cell membranes. Nature 387, 569–572 (1997). doi: 10.1038/42408
S.J. Singer, G.L. Nicolson, The fluid mosaic model of the structure of cell membranes. Science 175(4023), 720–731 (1972). doi: 10.1126/science.175.4023.720
B.-L. Song, N. Sever, R.A. DeBose-Boyd, Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Molecular Cell 19(6), 829–840 (2005). doi: 10.1016/j.molcel.2005.08.009
S.R. Spindler, R. Li, J.M. Dhahbi, A. Yamakawa, P. Mote, R. Bodmer, K. Ocorr, R.T. Williams, Y. Wang, K.P. Ablao, Statin treatment increases lifespan and improves cardiac health in Drosophila by decreasing specific protein prenylation. PLoS ONE 7(6), e39581 (2012). doi: 10.1371/journal.pone.0039581
R. Strasser, Biological significance of complex n-glycans in plants and their impact on plant physiology. Frontiers Plant Sci. 5(363), (2014). doi: 10.3389/fpls.2014.00363
L. Tagliavacca, T. Anelli, C. Fagioli, A. Mezghrani, E. Ruffato, R. Sitia, The making of a professional secretory cell: Architectural and functional changes in ER during B lymphocyte plasma cell differentiation. Biol. Chem. 384, 1273–1277 (2003). doi: 10.1515/BC.2003.141
B.P. Tu, J.S. Weissman, Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164(3), 341–346 (2004). doi: 10.1083/jcb.200311055
S. Wakabayashi, H. Yoshida, The essential biology of the endoplasmic reticulum stress response for structural and computational biologists. Comput. Struct. Biotechnol. J. 6, e201303010 (2013). doi: 10.5936/csbj.201303010
R. Zimmermann, S. Eyrisch, M. Ahmad, V. Helms, Protein translocation across the ER membrane. Biochim. Biophys. Acta 1808(3), 912–924 (2011). doi: 10.1016/j.bbamem.2010.06.015
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Buxbaum, E. (2015). Protein Transport Across Membranes. In: Fundamentals of Protein Structure and Function. Springer, Cham. https://doi.org/10.1007/978-3-319-19920-7_16
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DOI: https://doi.org/10.1007/978-3-319-19920-7_16
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