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- W1969443105 abstract "The Nobel Prize in physiology and medicine was in 1999 given for experiments allowing in vitro analysis of complicated biological processes – in particular for work on how proteins cross and become integrated into membrane/lipid bilayers. This work started with the formulation of the ‘signal hypothesis’ in the early 1970s. It stated that proteins have a signal that guides them to and determines whether they are completely translocated across the endoplasmic reti-culum (ER) membrane (secretory proteins) or inserted into the ER membrane (type I, II and multispan transmembrane proteins). Since lipids are hydrophobic and most proteins are hydrophilic, it was proposed that the ER membranes contain ‘translocons’ that provide an aqueous channel for the passage of proteins. Such translocons have been isolated; the major components in mammals of these channels are called Sec61p and Tram. However, while this answered how proteins cross the ER, information on how proteins such as receptors become inserted into the hydrophobic membranes remained obscure. Further progress was made possible by an elegant refinement of the in vitro system, leading to the formulation of the signal hypothesis. Indeed, one would like to probe whether the protein, during its insertion into the membrane, is in contact with other proteins (Sec61/Tram) or with lipids; to address this question, site-specific photocrosslinking was developed and used 1 Martoglio B. et al. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell. 1995; 81: 207-214 Abstract Full Text PDF PubMed Scopus (234) Google Scholar : by introducing a stop-codon at a desired position in the membrane protein that can be suppressed by tRNA charged with a photoactivatable alanine, such experiments became possible." @default.
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- W1969443105 date "2000-10-01" @default.
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- W1969443105 title "The construction of biological membranes" @default.
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- W1969443105 doi "https://doi.org/10.1016/s0962-8924(00)01842-0" @default.
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