Download Protein Transport into the Endoplasmic Reticulum by Richard Zimmermann PDF

By Richard Zimmermann

Protein shipping into the endoplasmic reticulum (ER) is only one element of the overall cellphone biology subject of intracellular protein sorting. This better photo additionally contains protein shipping into different organelles of the eukaryotic phone (chloroplasts, mitochondria, nucleus, peroxisomes), protein export from micro organism, vesicular shipping that offers to its ultimate vacation spot such a lot of what has been transported into the ER, and protein export from the ER that's linked to protein degradation (termed ERAD). through the years, protein delivery into the ER additionally has develop into a part of the search to appreciate a number of the roles of molecular chaperones lower than non-stress stipulations and of the ribosomal tunnel go out because the decisive website for molecular triage of nascent polypeptide chains.

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E) Directly after their cleavage from the precursor protein signal peptides may become degraded. This is probably true for most signal peptides but little is known about this process. 84-87 Intriguingly, it has recently been shown that intracellular peptides similar to those generated by the proteasome have the potential to affect cell signalling,88 implying an even bigger complexity of peptide mediated cellular processes. A detailed understanding of the molecular machinery involved in the turn over of signal peptides and the growing number of known post-targeting functions of signal Post-Targeting Functions of Signal Peptides 13 sequences will likely give new insight into functions that signal peptides can perform after their cleavage from the parent protein.

Hoch-Marchaim H, Weiss AM, Bar-Sinai A et al. The leader peptide of MMTV Env precursor localizes to the nucleoli in MMTV-derived T-cell lymphomas and interacts with nucleolar protein B23. Virology 2003; 313:22-32. 42. Dultz E, Hildenbeutel M, Martoglio B et al. The signal peptide of the mouse mammary tumor virus Rem protein is released from the endoplasmic reticulum membrane and accumulates in nucleoli. J Biol Chem 2008; 283:9966-76. 43. Kutay U, Guttinger S. Leucine-rich nuclear-export signals: born to be weak.

J Virol 2007; 81:5649-57. Agnihothram SS, York J, Nunberg JH. Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junin virus envelope glycoprotein complex. J Virol 2006; 80:5189-98. 14 Protein Transport into the Endoplasmic Reticulum 27. Schrempf S, Froeschke M, Giroglou T et al. Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity. J Virol 2007; 81:12515-24. 28. Eichler R, Lenz O, Strecker T et al.

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