Exchangers /

Current Topics in Membranes is targeted toward scientists and researchers in biochemistry and molecular and cellular biology, providing the necessary membrane research to assist them in understanding the current state and future prospects of a particular field. This volume on exchangers, in conjunct...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Άλλοι συγγραφείς: Bevensee, Mark O. (Επιμελητής έκδοσης)
Μορφή: Ηλ. βιβλίο
Γλώσσα:English
Έκδοση: Amsterdam : Elsevier, 2014.
Σειρά:Current topics in membranes ; volume 73.
Θέματα:
Διαθέσιμο Online:Full Text via HEAL-Link
Πίνακας περιεχομένων:
  • Front Cover; Exchangers; Copyright; Dedication; Contents; Contributors; Preface; Previous Volumes in Series; Chapter One: Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters; 1. Introduction; 2. Anion Exchanger 1 Structure and Function; 2.1. AE1 function; 2.2. AE1 structure; 3. AE1 Biosynthesis and N-glycosylation; 3.1. AE1 biosynthesis; 3.2. AE1 N-glycosylation; 4. Erythroid AE1 Protein Interactions; 4.1. Glycophorin A; 4.2. Proteins that interact with the cytosolic domain of AE1; 4.3. Carbonic anhydrase interaction with the C-terminal tail of AE1.
  • 5. Erythroid AE1-Associated Diseases5.1. AE1 Memphis; 5.2. AE1-associated blood group antigens; 5.3. Congenital dyserythropoietic anemia, type II (CDA II); 5.4. Southeast Asian Ovalocytosis; 5.5. Hereditary spherocytosis; 6. Retention and Rescue of AE1 Mutants; 6.1. Role of Glycophorin A in AE1 trafficking (Williamson and Toye, 2008); 6.2. AE1 biosynthesis during erythropoiesis; 7. Kidney AE1 Biogenesis, Interactors, and Associated Pathologies; 7.1. Kidney AE1 biosynthesis; 7.2. Kidney AE1 interactors; 7.3. Distal renal tubular acidosis (Yenchitsomanus et al., 2003).
  • 7.4. AE1 knockout mice develop dRTA7.5. Rescuing dRTA mutants; 8. SLC4 Family of Anion Transporters; 8.1. AE2 and AE3 structure, function, and disease; 8.2. Sodium-bicarbonate cotransporters; 9. The SLC26 (Sulp) Family of Anion Transporters; 9.1. SLC26 structure and function; 9.2. SLC26 family and disease; 10. Conclusions and Future Prospects; References; Chapter Two: Structural Dynamics and Regulation of the Mammalian SLC9A Family of Na+/H+ Exchangers; 1. Introduction; 2. Basic Functional Properties: Substrates, Driving Forces and Kinetics of SLC9As; 2.1. Pharmacological inhibitors of NHEs.
  • 3. Structural Organization and Dynamics of the TM Region of SLC9As3.1. Prokaryotic templates for understanding mammalian NHEs; 3.2. Mammalian SLC9A structures and models; 4. SLC9As Exist as Asymmetrical Homodimers in the Membrane; 4.1. pH-sensing site interrelated with the dimer interface; 4.2. Peptide models of NHE1 TMs; 4.3. Structure-based hypotheses for the mechanism of ion transport by NHEs; 4.4. The Phe-nomenon: A potential phenylalanine gate for ion transport; 5. The SLC9A C-Terminal Tail: Structure/Disorder, Interaction Partners, and Phosphorylation; 5.1. NHE1-binding partners.
  • 5.1.1. Interaction partners: Known structures of complexes5.2. Bioinformatical analyses and definition of subdomains of NHE1: ``Walking along the tail ́ ́; 5.3. ID as a conserved trait of the SLC9A family; 5.4. Subdomain-related interaction partners; 5.5. Interactions and regulation by ID in the SLC9A family; 5.6. Binding of protein kinases and phosphatases: Phosphorylation and dephosphorylation of NHE1; 6. Biophysics of SLC9A Function; 6.1. Proton sensing by NHEs: Allosteric H+-binding site versus high- and low-affinity dimer; 6.2. Volume sensing by NHEs.