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Structure paper

TitleStructural basis of TRPV5 regulation by physiological and pathophysiological modulators.
Journal, issue, pagesCell Rep, Vol. 39, Issue 4, Page 110737, Year 2022
Publish dateApr 26, 2022
AuthorsEdwin C Fluck / Aysenur Torun Yazici / Tibor Rohacs / Vera Y Moiseenkova-Bell /
PubMed AbstractTransient receptor potential vanilloid 5 (TRPV5) is a kidney-specific Ca-selective ion channel that plays a key role in Ca homeostasis. The basal activity of TRPV5 is balanced through activation by ...Transient receptor potential vanilloid 5 (TRPV5) is a kidney-specific Ca-selective ion channel that plays a key role in Ca homeostasis. The basal activity of TRPV5 is balanced through activation by phosphatidylinositol 4,5-bisphosphate (PI(4,5)P) and inhibition by Ca-bound calmodulin (CaM). Parathyroid hormone (PTH), the key extrinsic regulator of Ca homeostasis, increases the activity of TRPV5 via protein kinase A (PKA)-mediated phosphorylation. Metabolic acidosis leads to reduced TRPV5 activity independent of PTH, causing hypercalciuria. Using cryoelectron microscopy (cryo-EM), we show that low pH inhibits TRPV5 by precluding PI(4,5)P activation. We capture intermediate conformations at low pH, revealing a transition from open to closed state. In addition, we demonstrate that PI(4,5)P is the primary modulator of channel gating, yet PKA controls TRPV5 activity by preventing CaM binding and channel inactivation. Our data provide detailed molecular mechanisms for regulation of TRPV5 by two key extrinsic modulators, low pH and PKA.
External linksCell Rep / PubMed:35476976 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 4.2 Å
Structure data

25716

7t6j

EMDB-25716, PDB-7t6j:
Cryo-EM structure of TRPV5 at pH8 in nanodiscs
Method: EM (single particle) / Resolution: 3.2 Å

25717

7t6k

EMDB-25717, PDB-7t6k:
Cryo-EM structure of TRPV5 at pH6 in nanodiscs
Method: EM (single particle) / Resolution: 3.0 Å

25718

7t6l

EMDB-25718, PDB-7t6l:
Cryo-EM structure of TRPV5 at pH5 in nanodiscs
Method: EM (single particle) / Resolution: 3.7 Å

25719

7t6m

EMDB-25719, PDB-7t6m:
Cryo-EM structure of TRPV5 in nanodiscs with PI(4,5)P2 at pH6 state 1
Method: EM (single particle) / Resolution: 2.8 Å

25720

7t6n

EMDB-25720, PDB-7t6n:
Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 2
Method: EM (single particle) / Resolution: 2.9 Å

25721

7t6o

EMDB-25721, PDB-7t6o:
Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 3
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-25722: Cryo-EM structure of TRPV5 in detergent in the presence of PKA
Method: EM (single particle) / Resolution: 4.2 Å

25723

7t6p

EMDB-25723, PDB-7t6p:
Cryo-EM structure of TRPV5 T709D in nanodiscs
Method: EM (single particle) / Resolution: 2.8 Å

25724

7t6q

EMDB-25724, PDB-7t6q:
Cryo-EM structure of TRPV5 T709D with PI(4,5)P2 in nanodiscs
Method: EM (single particle) / Resolution: 3.4 Å

25725

7t6r

EMDB-25725, PDB-7t6r:
Cryo-EM structure of TRPV5 T709D in nanodiscs in the presence of Calmodulin
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-PIO:
[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate

Source
  • oryctolagus cuniculus (rabbit)
  • Mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / Calcium / Ion channel / Kidney

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