Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 146-150 |
| Number of pages | 5 |
| Journal | Trends in Cell Biology |
| Volume | 12 |
| Issue number | 3 |
| DOIs | |
| State | Published - Mar 1 2002 |
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ASJC Scopus subject areas
- Cell Biology
Cite this
Functional diversity of protein C-termini : More than zipcoding? / Chung, Jean Ju; Shikano, Sojin; Hanyu, Yoshiro; Li, Min.
In: Trends in Cell Biology, Vol. 12, No. 3, 01.03.2002, p. 146-150.Research output: Contribution to journal › Article
}
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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UR - http://www.scopus.com/inward/citedby.url?scp=0036498862&partnerID=8YFLogxK
U2 - 10.1016/S0962-8924(01)02241-3
DO - 10.1016/S0962-8924(01)02241-3
M3 - 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 -