SUMO Interacting Motifs: Structure and Function

Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-related protein family. SUMO modulates protein function through covalent conjugation to lysine residues in a large number of proteins. Once covalently conjugated to a protein, SUMO often regulates that protein’s function by recruit...

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Autores principales:	Tak-Yu Yau, William Sander, Christian Eidson, Albert J. Courey
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	SUMO SUMO interacting motif phase separation DNA repair host–pathogen interactions histones Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/751193b3c861494fbb8be161681366eb
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spelling	oai:doaj.org-article:751193b3c861494fbb8be161681366eb2021-11-25T17:07:39ZSUMO Interacting Motifs: Structure and Function10.3390/cells101128252073-4409https://doaj.org/article/751193b3c861494fbb8be161681366eb2021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4409/10/11/2825https://doaj.org/toc/2073-4409Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-related protein family. SUMO modulates protein function through covalent conjugation to lysine residues in a large number of proteins. Once covalently conjugated to a protein, SUMO often regulates that protein’s function by recruiting other cellular proteins. Recruitment frequently involves a non-covalent interaction between SUMO and a SUMO-interacting motif (SIM) in the interacting protein. SIMs generally consist of a four-residue-long hydrophobic stretch of amino acids with aliphatic non-polar side chains flanked on one side by negatively charged amino acid residues. The SIM assumes an extended β-strand-like conformation and binds to a conserved hydrophobic groove in SUMO. In addition to hydrophobic interactions between the SIM non-polar core and hydrophobic residues in the groove, the negatively charged residues in the SIM make favorable electrostatic contacts with positively charged residues in and around the groove. The SIM/SUMO interaction can be regulated by the phosphorylation of residues adjacent to the SIM hydrophobic core, which provide additional negative charges for favorable electrostatic interaction with SUMO. The SUMO interactome consists of hundreds or perhaps thousands of SIM-containing proteins, but we do not fully understand how each SUMOylated protein selects the set of SIM-containing proteins appropriate to its function. SIM/SUMO interactions have critical functions in a large number of essential cellular processes including the formation of membraneless organelles by liquid–liquid phase separation, epigenetic regulation of transcription through histone modification, DNA repair, and a variety of host–pathogen interactions.Tak-Yu YauWilliam SanderChristian EidsonAlbert J. CoureyMDPI AGarticleSUMOSUMO interacting motifphase separationDNA repairhost–pathogen interactionshistonesBiology (General)QH301-705.5ENCells, Vol 10, Iss 2825, p 2825 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	SUMO SUMO interacting motif phase separation DNA repair host–pathogen interactions histones Biology (General) QH301-705.5
spellingShingle	SUMO SUMO interacting motif phase separation DNA repair host–pathogen interactions histones Biology (General) QH301-705.5 Tak-Yu Yau William Sander Christian Eidson Albert J. Courey SUMO Interacting Motifs: Structure and Function
description	Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-related protein family. SUMO modulates protein function through covalent conjugation to lysine residues in a large number of proteins. Once covalently conjugated to a protein, SUMO often regulates that protein’s function by recruiting other cellular proteins. Recruitment frequently involves a non-covalent interaction between SUMO and a SUMO-interacting motif (SIM) in the interacting protein. SIMs generally consist of a four-residue-long hydrophobic stretch of amino acids with aliphatic non-polar side chains flanked on one side by negatively charged amino acid residues. The SIM assumes an extended β-strand-like conformation and binds to a conserved hydrophobic groove in SUMO. In addition to hydrophobic interactions between the SIM non-polar core and hydrophobic residues in the groove, the negatively charged residues in the SIM make favorable electrostatic contacts with positively charged residues in and around the groove. The SIM/SUMO interaction can be regulated by the phosphorylation of residues adjacent to the SIM hydrophobic core, which provide additional negative charges for favorable electrostatic interaction with SUMO. The SUMO interactome consists of hundreds or perhaps thousands of SIM-containing proteins, but we do not fully understand how each SUMOylated protein selects the set of SIM-containing proteins appropriate to its function. SIM/SUMO interactions have critical functions in a large number of essential cellular processes including the formation of membraneless organelles by liquid–liquid phase separation, epigenetic regulation of transcription through histone modification, DNA repair, and a variety of host–pathogen interactions.
format	article
author	Tak-Yu Yau William Sander Christian Eidson Albert J. Courey
author_facet	Tak-Yu Yau William Sander Christian Eidson Albert J. Courey
author_sort	Tak-Yu Yau
title	SUMO Interacting Motifs: Structure and Function
title_short	SUMO Interacting Motifs: Structure and Function
title_full	SUMO Interacting Motifs: Structure and Function
title_fullStr	SUMO Interacting Motifs: Structure and Function
title_full_unstemmed	SUMO Interacting Motifs: Structure and Function
title_sort	sumo interacting motifs: structure and function
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/751193b3c861494fbb8be161681366eb
work_keys_str_mv	AT takyuyau sumointeractingmotifsstructureandfunction AT williamsander sumointeractingmotifsstructureandfunction AT christianeidson sumointeractingmotifsstructureandfunction AT albertjcourey sumointeractingmotifsstructureandfunction
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SUMO Interacting Motifs: Structure and Function

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