NDLI: Shining a light on post-translational modification

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Shining a light on post-translational modification

Content Provider	PubMed Central
Author	Richards, Nigel G. J.
Copyright Year	2008
Abstract	Post-translational modification, such as phosphorylation or glycosylation, provides a mechanism for increasing the diversity of protein structures in the cell and regulating biological activity. In addition, such modifications may result in the localization of proteins to specific cellular organelles, with incorrect targeting being associated with a number of diseases. The simplest strategy to identify the functional importance of post-translational modifications is to use mutagenesis methods to replace the residue that is post-translationally modified by one that cannot undergo the relevant chemical transformation. Merely causing “loss of function” does not, however, address questions concerning how cellular function depends on the timing of post-translational changes and∕or the movement of modified proteins between organelles. The recent demonstration that genetically encoded “photocaged” proteins can be employed to resolve such issues therefore represents an exciting advance in this research area, and is an elegant illustration of the power of combining the power of chemical synthesis and methods for manipulating the biological machinery of protein synthesis.
Related Links	http://dx.doi.org/10.2976/1.2889161
Ending Page	60
Page Count	4
Starting Page	57
File Format	PDF
ISSN	19552068
e-ISSN	1955205X
Journal	HFSP Journal
Issue Number	2
Volume Number	2
Language	English
Publisher	HFSP Publishing
Publisher Date	2008-04-01
Access Restriction	Open
Rights Holder	HFSP Publishing
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Biochemistry, Genetics and Molecular Biology

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