Journal of Cell Science 115, e1001-e1001 (2002)
© 2002 The Company of Biologists Limited
Transmembrane protein biosynthesis
Getting transmembrane (TM) domain(s) into the right orientation during
biosynthesis is clearly essential for correct function of most integral
membrane proteins. But what are the factors that ensure this? And how
successful are current algorithms at predicting membrane protein topology from
amino acid sequence alone — particularly if the protein has multiple TM
segments? In a Commentary on p.
2003, Carolyn Ott and Vishwanath Lingappa review work that is
shedding light on the role of intra- and inter-protein interactions in
regulating integral membrane protein topology. Intraprotein interactions
include those involving `strong orientation effectors', such as TM domain 8 of
the model protein band 3, which forces the integration of the preceding TM
domain. Correct orientation of other proteins (e.g. IgM) requires interprotein
interactions, which involve trans-acting factors such as translation accessory
factors (TrAFs) or the stop transfer effector (STE) receptor. Indeed, the
complexity of membrane protein biogenesis underlines the need for caution when
topology prediction algorithms are used, particularly given that several
proteins are synthesized in several distinct topological forms.
Related articles in JCS:
- Integral membrane protein biosynthesis: why topology is hard to predict
- Carolyn M. Ott and Vishwanath R. Lingappa
JCS 2002 115: 2003-2009.
[Abstract]
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