TY - JOUR
T1 - Functional diversity of protein C-termini
T2 - More than zipcoding?
AU - Chung, Jean Ju
AU - Shikano, Sojin
AU - Hanyu, Yoshiro
AU - Li, Min
PY - 2002/3/1
Y1 - 2002/3/1
N2 - The carboxylated (C)-terminus of proteins, which includes the single terminal α-carboxyl group and preceding residues, is uniquely positioned to serve as a recognition signature for a variety of cell-biological processes, including protein targeting, subcellular anchoring and the static and dynamic formation of macromolecular complexes. The terminal sequence motifs can be processed by posttranslational modifications, thereby providing a means to increase sequence diversity and to regulate interactions. Several classes of protein domains have been identified that are either designed for or are capable of interacting with protein C-termini - these include PDZ and TPR domains. The interactions between these protein domains and various terminal epitopes play an important role in specifying cell-biological functions. The combination of diversity and the plasticity of the chemistry of C-termini provides mechanisms for spatial and temporal specificity that are exploited by a variety of biological processes, ranging from specifying prokaryotic protein degradation to nucleating mammalian neuronal signaling complexes. Understanding the diverse functions of protein C-termini might also provide an important indexing criterion for functional proteomics.
AB - The carboxylated (C)-terminus of proteins, which includes the single terminal α-carboxyl group and preceding residues, is uniquely positioned to serve as a recognition signature for a variety of cell-biological processes, including protein targeting, subcellular anchoring and the static and dynamic formation of macromolecular complexes. The terminal sequence motifs can be processed by posttranslational modifications, thereby providing a means to increase sequence diversity and to regulate interactions. Several classes of protein domains have been identified that are either designed for or are capable of interacting with protein C-termini - these include PDZ and TPR domains. The interactions between these protein domains and various terminal epitopes play an important role in specifying cell-biological functions. The combination of diversity and the plasticity of the chemistry of C-termini provides mechanisms for spatial and temporal specificity that are exploited by a variety of biological processes, ranging from specifying prokaryotic protein degradation to nucleating mammalian neuronal signaling complexes. Understanding the diverse functions of protein C-termini might also provide an important indexing criterion for functional proteomics.
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U2 - 10.1016/S0962-8924(01)02241-3
DO - 10.1016/S0962-8924(01)02241-3
M3 - Review article
C2 - 11859027
AN - SCOPUS:0036498862
VL - 12
SP - 146
EP - 150
JO - Trends in Cell Biology
JF - Trends in Cell Biology
SN - 0962-8924
IS - 3
ER -