Chapter 26

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von Heijne, G. (1998). Life and death of a signal peptide. Nature, 396, 111-12 [DOI: 10.1038/24036].
A News and Views article on signal peptide cleavage as the transported polypeptide emerges into the lumen of the ER.

Matlack, K. E. S., Mothes, W., and Rapoport, T. A. (1998). Protein translocation: tunnel vision. Cell 92, 381-90 [DOI: 10.1016/S0092-8674(00)80930-7] [PubMed: 9476897].
Refers to protein transport through the ER membrane.

Bernstein, P. (2000). Molecular trafficking. Essays Biochem., 36, 1-129.
A complete issue devoted to 10 reviews on protein targeting.

Eichler, J. and Irihimovitch, V. (2003). Move it on over: getting proteins across biological membranes. BioEssays, 25, 1154-7 [DOI: 10.1002/bies.10382] [PubMed: 14635250].
Two distinct modes mediated by ‘translocons’ - the macro molecular complex that translocates proteins across membranes.

Golgi

Short, B. and Barr, F. A. (2000). The Golgi apparatus. Curr. Biol., 10, R583-5 [DOI: 10.1016/S0960-9822(00)00644-8].
Short review

Lysosomes

Neufeld, E. F. (1991). Lysosomal storage diseases. Annu. Rev. Biochem., 60, 257-80 [DOI: 10.1146/annurev.bi.60.070191.001353].
Reviews general principles and specific diseases

Bonifacino, J. S. and Traub, L. M. (2003). Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem., 72, 395-447 [DOI: 10.1146/annurev.biochem.72.121801.161800].
A research-level review

COP-coated vesicle formation and targeting

Edwardson, J. M. (1998). Membrane fusion: all done with SNARE pins. Curr. Biol., 8, R390-3 [DOI: 10.1016/S0960-9822(98)70245-3].
All about SNARE proteins and transport vesicle targeting

Lowe, M. (2000). Membrane transport: tethers and TRAPPs. Curr. Biol., 10, R407-9 [DOI: 10.1016/S0960-9822(00)00505-4].
Brief summary of v-SNARES and t-SNARES

Mallabiabarrena, A. and Malhotra, V. (1995). Vesicle biogenesis: the coat connection. Cell 83, 667-9 [DOI: 10.1016/0092-8674(95)90177-9] [PubMed: 8521481].
A minireview that discusses why different coat proteins are used for the transport of vesicles.

Schmid, S. L. and Damke, H. (1995). Coated vesicles: a diversity of form and function. FASEB J., 9, 1445-53.
Reviews the different ways in which coated vesicles are budded off from the Golgi and other membranes.

Schekman, R. and Orci, L. (1996). Coat proteins and vesicle budding. Science, 271, 1526-33 [DOI: 10.1126/science.271.5255.1526] [PubMed: 8599108].
A review of vesicle transport and their role in sorting of proteins.

Wieland, F. and Harte, C. (1999). Mechanisms of vesicle formation: insights from the COP system. Curr. Opin. Cell Biol., 11, 440-6 [DOI: 10.1016/S0955-0674(99)80063-5].
Discussing formation of transport vesicles

Clathrin

Marsh, M. and McMahon, H. T. (1999). The structural era of endocytosis. Science, 285, 215-19 [DOI: 10.1126/science.285.5425.215] [PubMed: 10398591].
A concise review of clathrin coat assembly.

Peroxisomes

Shimozawa, N., et al. (1992). A human gene responsible for Zellweger syndrome that affects peroxisome assembly. Science, 255, 1132-4 [DOI: 10.1126/science.1546315] [PubMed: 1546315].
Shows that the Zellweger syndrome primary cause is a defect in the synthesis of a peroxisome assembly protein.

McNew, J. A. and Goodman, J. M. (1995). The targeting and assembly of peroxisomal proteins: some old rules do not apply. Trends Biochem. Sci., 21, 54-8 [DOI: 10.1016/0968-0004(96)80866-8].
Reviews evidence that folded proteins are imported into peroxisomes as such.

Subramani, S., Koller, A., and Snyder, W. B. (2000). Import of peroxisomal matrix and membrane proteins. Annu. Rev. Biochem., 69, 399-418 [DOI: 10.1146/annurev.biochem.69.1.399].
Comprehensive review of peroxisomal biogenesis

Mitochondria

Pfanner, N. and Meijer, M. (1997). Mitochondrial biogenesis: the TOM and TIM machine. Curr. Biol., 7, R100-3 [DOI: 10.1016/S0960-9822(06)00048-0].
Reviews the field

Koehler, C. M., Merchant, S., and Schatz, G. (1998). How membrane proteins travel across the mitochondrial intermembrane space. Trends Biochem. Sci., 24, 428-32 [DOI: 10.1016/S0968-0004(99)01462-0].
Deals with the special proteins needed to conduct hydrophobic proteins across the aqueous intermembrane space. Deficiencies in these lead to blindness and deafness.

Paschen, S. A. and Neupert, W. (2001). Protein import into mitochondria. IUBMB Life. 52, 101-12 [DOI: 10.1080/15216540152845894] [PubMed: 11798021].

Neupert, W. and Herrmann, J. M. (2007). Translocation of proteins into mitochondria. Annu. Rev. Biochem., 76, 723-49 [DOI: 10.1146/annurev.biochem.76.052705.163409].

Schatz, G. (2007). The Magic Garden. Annu. Rev. Biochem., 76, 673-678 [DOI: 10.1146/annurev.biochem.76.060806.091141].
A highly readable personal review of mitochondrial assembly and how the field, in which the author has played a major part, has developed.

Nucleus

Mattaj, I. W. and Englmeir, L. (1998). Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem, 67, 265-306 [DOI: 10.1146/annurev.biochem.67.1.265].
A comprehensive review

Mattaj, I. W. and Conti, E. (1999). Snail mail to the nucleus. Nature, 399, 208-10 [DOI: 10.1038/20322] [PubMed: 10353239].
Concise News and Views article describing the mechanism of nuclear-cytoplasmic transport.

Blobel, G. and Wozniak, R. W. (2000). Proteomics for the pore. Nature, 403, 835-6 [DOI: 10.1038/35002687] [PubMed: 10706261].
News and Views article describing work by Rout and colleagues, which gives a complete structure of the nuclear pore.

Weis, K. (2003). Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112, 441-51 [DOI: 10.1016/S0092-8674(03)00082-5] [PubMed: 12600309].

Burke, B. (2006). Nuclear pore complex models gel. Science, 314, 766-7 [DOI: 10.1126/science.1135739] [PubMed: 17082440].
A postulated mechanism for nuclear pore transport.

Beck, M., Lucic, V., Forster, F., Baumeister, W., and Medalia, O. (2007). Snapshots of nuclear pore complexes in action captured by cryoelectron tomography. Nature, 449, 611-5 [DOI: 10.1038/nature06170] [PubMed: 17851530].

Protein glycosylation

Abeijon, C. and Hirschberg, C. B. (1992). Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem. Sci., 17, 32-6 [DOI: 10.1016/0968-0004(92)90424-8].
Reviews the different protein glycosylation reactions occurring in the endoplasmic reticulum.

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