ArticleBlood cells, molecules & diseases
Chemical crosslinking studies with the mouse Kcc1 K-Cl cotransporter.
Article in Blood cells, molecules & diseases. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Sheep erythrocyte potassium locus highlights MYADM family regulation of electroneutral potassium chloride cotransporters (KCC).BMC genomics · 2026Article
- Carfilzomib in multiple myeloma: unraveling cardiac toxicities - from mechanisms to diagnosis and management.Frontiers in pharmacology · 2025Review
- Reciprocal Regulation of KCC2 Trafficking and Synaptic Activity.Frontiers in cellular neuroscience · 2019Review
- Molecular and evolutionary insights into the structural organization of cation chloride cotransporters.Frontiers in cellular neuroscience · 2014Review
- Current view on the functional regulation of the neuronal K(+)-Cl(-) cotransporter KCC2.Frontiers in cellular neuroscience · 2014Review
- RNA binding by the NS3 protease of the hepatitis C virus.Virus research · 2012Article
- ReCLIP (reversible cross-link immuno-precipitation): an efficient method for interrogation of labile protein complexes.PloS one · 2011Article
- Differences in the large extracellular loop between the K(+)-Cl(-) cotransporters KCC2 and KCC4.The Journal of biological chemistry · 2010Article
- The biogenesis of potassium transporters: implications of disease-associated mutations.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Oligomerization, function, and regulation of unmodified mouse Kcc1 K-Cl cotransporter were studied by chemical crosslinking. Treatment of Xenopus oocytes and 293T cells expressing K-Cl cotransporter Kcc1 with several types of chemical cross-linkers shifted Kcc1 polypeptide to higher molecular weight forms. More extensive studies were performed with the amine-reactive disuccinyl suberate (DSS) and with the sulfhydryl-reactive bis-maleimidohexane (BMH). Kcc1 cross-linking was time-dependent in intact oocytes, and was independent of protein concentration in detergent lysates from oocytes or 293T cells. Kcc1 cross-linking by the cleavable cross-linker DTME was reversible. The N-terminal and C-terminal cytoplasmic tails of Kcc1 were not essential for Kcc1 crosslinking. PFO-PAGE and gel filtration revealed oligomeric states of uncrosslinked KCC1 corresponding in mobility to that of cross-linked protein. DSS and BMH each inhibited KCC1-mediated (86)Rb(+) uptake stimulated by hypotonicity or by N-ethylmaleimide (NEM) without reduction in nominal surface abundance of KCC1. These data add to evidence supporting the oligomeric state of KCC polypeptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.