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Small Ubiquitin-Like Modifiers and Other Ubiquitin-Like Proteins

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Post-Translational Modifications in Health and Disease

Part of the book series: Protein Reviews ((PRON,volume 13))

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Abstract

SUMOs are Small Ubiquitin-like Modifiers that are covalently conjugated to extensive sets of target proteins in cells to regulate their activity. A properly functioning sumoylation system is essential for eukaryotic life. The system comprises a set of conjugating enzymes known as E1, E2 and E3s and a set of deconjugating enzymes known as SENPs. Three mammalian SUMO family members have been identified, SUMO-1, SUMO-2 and SUMO-3. Sumoylation is involved in virtually all cellular processes including transcription, DNA damage response pathways, transport, ribosome biogenesis, pre-mRNA splicing, RNA editing and the cell cycle. Similar to ubiquitin, SUMOs form chains via internal sumoylation sites present in the flexible N-terminal parts of SUMO-2, SUMO-3 and the single SUMO family member in S. cerevisiae SMT3. SUMO-interacting proteins bind to mono- or poly-sumoylated proteins in a non-covalent manner to regulate the fate of sumoylated proteins. Sumoylation acts in concert with other post-translational modifications such as phosphorylation, acetylation and ubiquitination. In addition to SUMOs, the ubiquitin family consists of ISG15, NEDD8, ATG8, ATG12, FUBI, URM1, UFM1, FAT10, HUB1 and PUP. These protein modifiers play important roles in immunity, autophagy, ribosome biogenesis and other processes.

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Abbreviations

Aos1:

Activation of Smt3p

ATG8:

Autophagy-related protein 8

ATG12:

Autophagy-related protein 12

E1:

SUMO activating enzyme

E2:

SUMO protein carrier protein

E3:

SUMO ligase

FAT10:

Ubiquitin-like protein FAT10

FUBI:

Ubiquitin-like protein FUBI

GMP1:

GAP-modifying protein 1

HDAC:

Histone deacetylase

HECT:

Homologous to the E6-AP carboxyl terminus

HIF:

Hypoxia-inducible factor

HUB1:

Ubiquitin-like modifier HUB1

IκBα:

NFκB inhibitor α

IR:

Internal repeats

ISG15:

Interferon-stimulated gene 15

Mdm2:

Mouse double minute 2

NDSM:

Negatively charged amino acid-dependent sumoylation motif

NEDD8:

Neural precursor cell expressed developmentally down-regulated protein 8

NFκB:

Nuclear factor κB

NPC:

Nuclear pore complex

Pc2:

Polycomb protein 2

PDSM:

Phosphorylation-dependent sumoylation motif

PIAS:

Protein inhibitor of activated STAT

PIC1:

PML-interacting clone 1

PML:

Promyelocytic leukemia protein

PUP:

Prokaryotic ubiquitin-like protein

RanBP:

Ran-binding protein

RanGAP:

Ran GTPase-activating protein

RING:

Really interesting new gene

RNF4:

RING finger protein 4

SAE:

SUMO activating enzyme

SENP:

SUMO protease

SILAC:

Stable-isotope labeling by amino acids in cell culture

SIM:

SUMO interaction motif

Siz:

SAP and Miz-finger domain-containing protein 1

SMT3:

Suppressor of mif two 3

STAT:

Signal transducer and activator of transcription

SUMO:

Small ubiquitin-like modifier

TAF:

TBP-associated factor

TBP:

TATA box binding protein

TDG:

Thymine-DNA glycosylase

Uba2:

Ubiquitin-activating enzyme E1-like

Ubc9:

Ubiquitin carrier protein 9

UBL1:

Ubiquitin-like protein 1

UFM1:

Ubiquitin-fold modifier 1

Ulp:

Ubiquitin-like-specific protease

URM1:

Ubiquitin-related modifier 1

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Acknowledgments

We are grateful to Joost Schimmel, Ivo Hendriks and Sarah Sparks for critically reading the manuscript. We thank Ivo Hendriks for preparing Table 13.1. We apologise to colleagues whose work was not cited due to space constrains. Research in the laboratory of ACOV is supported by the Netherlands Organisation for Scientific Research (NWO).

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  1. Department of Molecular Cell Biology, Leiden University Medical Center, 9600, Mailzone S-1-P, 2300 RC, Leiden, The Netherlands

    Alfred C. O. Vertegaal

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  1. Martijn van Hagen
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Correspondence to Alfred C. O. Vertegaal .

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  1. Depto. Quimica Inorganica, Universidad Murcia, Murcia, Spain

    Cecilio J. Vidal

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van Hagen, M., Vertegaal, A.C.O. (2011). Small Ubiquitin-Like Modifiers and Other Ubiquitin-Like Proteins. In: Vidal, C. (eds) Post-Translational Modifications in Health and Disease. Protein Reviews, vol 13. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6382-6_13

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