title: Ubiquitin Ligases and Deubiquitinating Enzymes in CD4+ T Cell Effector Fate Choice and Function.
abstract: The human body is exposed to potentially pathogenic microorganisms at barrier sites such as the skin, lungs, and gastrointestinal tract. To mount an effective response against these pathogens, the immune system must recruit the right cells with effector responses that are appropriate for the task at hand. Several types of CD4(+) T cells can be recruited, including Th cells (Th1, Th2, and Th17), T follicular helper cells, and regulatory T cells. These cells help to maintain normal immune homeostasis in the face of constantly changing microbes in the environment. Because these cells differentiate from a common progenitor, the composition of their intracellular milieu of proteins changes to appropriately guide their effector function. One underappreciated process that impacts the levels and functions of effector fate-determining factors is ubiquitylation. This review details our current understanding of how ubiquitylation regulates CD4(+) T cell effector identity and function.
authors.affiliation: Medical Scientist Training Program, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104; and.
authors.forename: Awo A K
authors.identifier: 0000-0001-9815-1445
authors.initials: AA
authors.lastname: Layman
authors.affiliation: Department of Pathology, Children's Hospital of Philadelphia and Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104 paulao@mail.med.upenn.edu.
authors.forename: Paula M
authors.identifier: 0000-0002-0455-3767
authors.initials: PM
authors.lastname: Oliver
mesh_terms: D000818:Animals; D002454:Cell Differentiation; D019070:Cell Lineage; D004781:Environmental Exposure; D041981:Gastrointestinal Tract / Q000276:immunology*; D006706:Homeostasis; D006801:Humans; D007109:Immunity; D007239:Infections / Q000276:immunology*; D008168:Lung / Q000276:immunology*; D012867:Skin / Q000276:immunology*; D016176:T-Lymphocyte Subsets / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D044767:Ubiquitin-Protein Ligases