Moving the Cellular Peptidome by Transporters

Frontiers in Cell and Developmental Biology
Rupert Abele, Robert Tampé

Abstract

Living matter is defined by metastability, implying a tightly balanced synthesis and turnover of cellular components. The first step of eukaryotic protein degradation via the ubiquitin-proteasome system (UPS) leads to peptides, which are subsequently degraded to single amino acids by an armada of proteases. A small fraction of peptides, however, escapes further cytosolic destruction and is transported by ATP-binding cassette (ABC) transporters into the endoplasmic reticulum (ER) and lysosomes. The ER-resident heterodimeric transporter associated with antigen processing (TAP) is a crucial component in adaptive immunity for the transport and loading of peptides onto major histocompatibility complex class I (MHC I) molecules. Although the function of the lysosomal resident homodimeric TAPL-like (TAPL) remains, until today, only loosely defined, an involvement in immune defense is anticipated since it is highly expressed in dendritic cells and macrophages. Here, we compare the gene organization and the function of single domains of both peptide transporters. We highlight the structural organization, the modes of substrate binding and translocation as well as physiological functions of both organellar transporters.

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Citations

Jun 23, 2020·Annual Review of Biochemistry·Christoph Thomas, Robert Tampé
Dec 24, 2018·Journal of Peptide Science : an Official Publication of the European Peptide Society·Anna FilippovaIgor Fesenko
Apr 16, 2019·Current Opinion in Oncology·James W Mier
Oct 6, 2020·F1000Research·Anita J ZaitouaMalini Raghavan
Nov 9, 2018·Expert Review of Proteomics·Eric A Wilson, Karen S Anderson
Mar 11, 2021·Current Opinion in Immunology·Christoph Thomas, Robert Tampé

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Methods Mentioned

BETA
X-ray
NMR
fluorescence correlation spectroscopy

Software Mentioned

Clustal Omega

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