Academic Journal
Dimerization in the SLC12 family: Structural and biochemical perspectives.
| Τίτλος: | Dimerization in the SLC12 family: Structural and biochemical perspectives. |
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| Συγγραφείς: | Náplavová A; Danish Research Institute of Translational Neuroscience - DANDRITE, Nordic-EMBL Partnership for Molecular Medicine. Department of Molecular Biology and Genetics, Aarhus University, Denmark., Nissen P; Danish Research Institute of Translational Neuroscience - DANDRITE, Nordic-EMBL Partnership for Molecular Medicine. Department of Molecular Biology and Genetics, Aarhus University, Denmark., Flygaard RK; Department of Molecular Biology and Genetics, Aarhus University, Denmark. Electronic address: rkf@mbg.au.dk. |
| Πηγή: | Journal of structural biology [J Struct Biol] 2026 Sep; Vol. 218 (3), pp. 108356. Date of Electronic Publication: 2026 Aug 11. |
| Τύπος έκδοσης: | Journal Article; Review |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Academic Press Country of Publication: United States NLM ID: 9011206 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-8657 (Electronic) Linking ISSN: 10478477 NLM ISO Abbreviation: J Struct Biol Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: San Diego : Academic Press, c1990- |
| Ιατρικοί όροι (MeSH): | Protein Multimerization* , Solute Carrier Family 12*, Humans ; Cryoelectron Microscopy ; Protein Conformation ; Models, Molecular ; Animals ; Ion Transport |
| Περίληψη: | Solute carrier proteins (SLCs) are essential membrane protein transporters of small solutes. Among them, the SLC12 family is known to facilitate transport of ions. Members of the SLC12 family ensure cell homeostasis by co-transporting chloride alongside sodium and/or potassium across the plasma membrane. The majority of SLC12 proteins are well described, and a recent surge in structural studies facilitated by cryo-electron microscopy revealed molecular details of their function. These include multiple conformations of the transporters, covering a range of functional states and providing a window into the ion transport mechanism. Yet, only limited knowledge exists regarding their dimerization or higher order oligomerization and its role in regulation, despite SLC12 proteins consistently operating as dimers. In this review, we highlight the structural knowledgebase established in recent years and summarize the varying dimerization mechanisms. Altogether, it is becoming increasingly clear that large conformational changes in dimeric arrangements deserve attention, alongside other understudied areas like lipid interactions, nucleotide or N-terminal binding to the dimerization domains, and potential roles of the less described member SLC12A9. (Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.) |
| Competing Interests: | Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. |
| Contributed Indexing: | Keywords: Cation-chloride cotransporters; Heterodimerization; Homodimerization; SLC12; SLC12 dimerization |
| Substance Nomenclature: | 0 (Solute Carrier Family 12) |
| Entry Date(s): | Date Created: 20260811 Date Completed: 20260903 Latest Revision: 20260903 |
| Update Code: | 20260904 |
| DOI: | 10.1016/j.jsb.2026.108356 |
| PMID: | 42580644 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 1095-8657 |
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| DOI: | 10.1016/j.jsb.2026.108356 |