Title

The Carboxy-Terminus, a Key Regulator of Protein Function

Document Type

Article

Publication Date

5-20-2019

Publication Title

Critical Reviews in Biochemistry and Molecular Biology

Volume

54

Issue

2

First page number:

85

Last page number:

102

Abstract

All proteins end with a carboxyl terminus that has unique biophysical properties and is often disordered. Although there are examples of important C-termini functions, a more global role for the C-terminus is not yet established. In this review, we summarize research on C-termini, a unique region in proteins that cells exploit. Alternative splicing and proteolysis increase the diversity of proteins and peptides in cells with unique C-termini. The C-termini of proteins contain minimotifs, short peptides with an encoded function generally characterized as binding, posttranslational modifications, and trafficking. Many of these activities are specific to minimotifs on the C-terminus. Approximately 13% of C-termini in the human proteome have a known minimotif, and the majority, if not all of the remaining termini have conserved motifs inferring a function that remains to be discovered. C-termini, their predictions, and their functions are collated in the C-terminome, Proteus, and Terminus Oriented Protein Function INferred Database (TopFIND) database/web systems. Many C-termini are well conserved, and some have a known role in health and disease. We envision that this summary of C-termini will guide future investigation of their biochemical and physiological significance.

Keywords

C-terminus, minimotifs; C-terminome; Short linear motifs; Posttranslational modification; Trafficking; C-terminal minimotifs

Disciplines

Biochemistry | Biology | Molecular Biology

Language

English

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