Sodium-Coupled Substrate Translocation Mechanism via the Sodium/Betaine Symporter
نویسندگان
چکیده
منابع مشابه
Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.
Significant advances have been made in recent years in characterizing neurotransmitter:sodium symporter (NSS) family structure and function. Yet, many time-resolved events and intermediates that control the various stages of transport cycle remain to be elucidated. Whether NSSs harbor one or two sites for binding their substrates (neurotransmitters or amino acids), and what the role of the seco...
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The movement of a variety of species from the iodine-rich environment of the sea to the relatively iodine-deficient land has necessitated the development of mechanisms which will trap more efficiently inorganic iodide (I – ) necessary for the formation of thyroid hormones (Venturi et al. , 2000). In man as in other mammals iodide uptake by the thyroid is mediated via a TSHdependent transmembran...
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PURPOSE Human sodium/iodide symporter (hNIS) protein is a membrane glycoprotein that transports iodide ions into thyroid cells. The function of this membrane protein is closely regulated by post-translational glycosylation. In this study, we measured glycosylation-mediated changes in subcellular location of hNIS and its function of iodine uptake. METHODS HeLa cells were stably transfected wit...
متن کاملSodium-Assisted Formation of Binding and Traverse Conformations of the Substrate in a Neurotransmitter Sodium Symporter Model
Therapeutics designed to increase synaptic neurotransmitter levels by inhibiting neurotransmitter sodium symporters (NSSs) classify a strategic approach to treat brain disorders such as depression or epilepsy, however, the critical elementary steps that couple downhill flux of sodium to uphill transport of neurotransmitter are not distinguished as yet. Here we present modelling of NSS member ne...
متن کاملSimulations of the alternating access mechanism of the sodium symporter Mhp1.
Sodium coupled cotransporters of the five-helix inverted repeat (5HIR) superfamily use an alternating access mechanism to transport a myriad of small molecules across the cell membrane. One of the primary steps in this mechanism is the conformational transition from a state poised to bind extracellular substrates to a state that is competent to deliver substrate to the cytoplasm. Here, we const...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2011
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.12.942