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Structural Asymmetry of AcrB Trimer Suggests a Peristaltic Pump Mechanism
- M. Seeger, A. Schiefner, T. Eicher, F. Verrey, K. Diederichs, K. M. Pos
- Chemistry, MedicineScience
- 1 September 2006
A crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups reveals three different monomer conformations representing consecutive states in a transport cycle, implying an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.
Epithelial sodium channel regulated by aldosterone-induced protein sgk.
- S. Chen, A. Bhargava, +6 authors D. Pearce
- Biology, MedicineProceedings of the National Academy of Sciences…
- 2 March 1999
Sgk (serum and glucocorticoid-regulated kinase), a member of the serine-threonine kinase family, is identified as an aldosterone-induced regulator of ENaC activity, suggesting that sgk plays a central role in ald testosterone regulation of Na+ absorption and thus in the control of extracellular fluid volume, blood pressure, and sodium homeostasis.
Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop
- T. Eicher, Hi-jea Cha, +8 authors K. M. Pos
- Biology, MedicineProceedings of the National Academy of Sciences
- 26 March 2012
High resolution structures are reported of AcrB/designed ankyrin repeat protein (DARPin) complexes with bound minocycline or doxorubicin and transport seems to be a stepwise process of initial drug uptake in the access pocket of the L monomer and subsequent accommodation of the drug in the deep binding pocket during the L to T transition.
ACE2 links amino acid malnutrition to microbial ecology and intestinal inflammation
The results identify ACE2 as a key regulator of dietary amino acid homeostasis, innate immunity, gut microbial ecology, and transmissible susceptibility to colitis, providing a molecular explanation for how amino acid malnutrition can cause intestinal inflammation and diarrhoea.
LAT2, a New Basolateral 4F2hc/CD98-associated Amino Acid Transporter of Kidney and Intestine*
- G. Rossier, C. Meier, +4 authors L. Kühn
- Biology, MedicineThe Journal of Biological Chemistry
- 3 December 1999
It is proposed that LAT1 is involved in cellular amino acid uptake, whereas LAT2 plays a role in epithelial amino acid (re)absorption in vertebrate gpaATs.
Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
The permease-related protein E16 is identified as the first light chain of h4F2hc and it is shown that the resulting heterodimeric complex mediates L-type amino-acid transport.
Amino acid transport of y+L‐type by heterodimers of 4F2hc/CD98 and members of the glycoprotein‐associated amino acid transporter family
- R. Pfeiffer, G. Rossier, B. Spindler, C. Meier, L. Kühn, F. Verrey
- Biology, MedicineThe EMBO journal
- 4 January 1999
The y+LAT1–4F2hc heterodimer, besides participating in amino acid uptake/secretion in many cell types, is the basolateral amino acid exchanger involved in transepithelial reabsorption of cationic amino acids; hence, its defect might be the cause of the human genetic disease lysinuric protein intolerance.
Activation of system L heterodimeric amino acid exchangers by intracellular substrates
The two system L amino acid transporters that are implicated in cell growth and transcellular transport are obligatory exchangers with relatively symmetrical substrate selectivities but strongly asymmetrical substrate affinities such that the intracellular amino acid concentration controls their activity.
Aldosterone induces rapid apical translocation of ENaC in early portion of renal collecting system: possible role of SGK.
- J. Loffing, M. Zečević, +6 authors F. Verrey
- Biology, MedicineAmerican journal of physiology. Renal physiology
- 1 April 2001
It is shown by real-time RT-PCR and immunofluorescence that an aldosterone injection in adrenalectomized rats induces alpha-ENaC subunit expression along the entire ASDN within 2 h, whereas beta- and gamma- ENaC are constitutively expressed.
System L: heteromeric exchangers of large, neutral amino acids involved in directional transport
- F. Verrey
- Chemistry, MedicinePflügers Archiv
- 1 February 2003
Net directional transport of large, neutral amino acids by system L depends on the parallel expression of a unidirectional transporter with overlapping selectivity that provides/recycles amino acids that drive system L exchange function.