Functional diversity of protein C-termini: More than zipcoding?

Jean Ju Chung, Sojin Shikano, Yoshiro Hanyu, Min Li

Research output: Contribution to journalReview articlepeer-review


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 languageEnglish (US)
Pages (from-to)146-150
Number of pages5
JournalTrends in Cell Biology
Issue number3
StatePublished - Mar 1 2002

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Functional diversity of protein C-termini: More than zipcoding?'. Together they form a unique fingerprint.

Cite this