Protein Structure and Modification of Aquaporins

Xiong, Mengyao; Li, Chunling; Wang, Weidong; Yang, Baoxue

doi:10.1007/978-981-19-7415-1_2

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2023

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“…TM1–3 and TM4–6 display obverse symmetry and fold in a way that two loops (loops B and E) come together to form a single aqueous pore through the lipid bilayer, basically corresponding to a seventh transmembrane domain (the ‘hourglass’; Walz et al., 1997). Almost invariably each of the B and E loops contains an Asp‐Pro‐Ala motif (NPA box) at the centre of the pore (Xiong et al., 2023) (Fig. 2 A ).…”

Section: Introductionmentioning

confidence: 99%

Many kinases for controlling the water channel aquaporin‐2

Kharin

Klussmann

2023

The Journal of Physiology

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Aquaporin‐2 (AQP2) is a member of the aquaporin water channel family. In the kidney, AQP2 is expressed in collecting duct principal cells where it facilitates water reabsorption in response to antidiuretic hormone (arginine vasopressin, AVP). AVP induces the redistribution of AQP2 from intracellular vesicles and its incorporation into the plasma membrane. The plasma membrane insertion of AQP2 represents the crucial step in AVP‐mediated water reabsorption. Dysregulation of the system preventing the AQP2 plasma membrane insertion causes diabetes insipidus (DI), a disease characterised by an impaired urine concentrating ability and polydipsia. There is no satisfactory treatment of DI available. This review discusses kinases that control the localisation of AQP2 and points out potential kinase‐directed targets for the treatment of DI. image

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Section: Introductionmentioning

confidence: 99%