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TitleCryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7.
Journal, issue, pagesLife Sci Alliance, Vol. 5, Issue 11, Year 2022
Publish dateJul 6, 2022
AuthorsYong Zi Tan / Yazan M Abbas / Jing Ze Wu / Di Wu / Kristine A Keon / Geoffrey G Hesketh / Stephanie A Bueler / Anne-Claude Gingras / Carol V Robinson / Sergio Grinstein / John L Rubinstein /
PubMed AbstractV-ATPases are rotary proton pumps that serve as signaling hubs with numerous protein binding partners. CryoEM with exhaustive focused classification allowed detection of endogenous proteins ...V-ATPases are rotary proton pumps that serve as signaling hubs with numerous protein binding partners. CryoEM with exhaustive focused classification allowed detection of endogenous proteins associated with porcine kidney V-ATPase. An extra C subunit was found in ∼3% of complexes, whereas ∼1.6% of complexes bound mEAK-7, a protein with proposed roles in dauer formation in nematodes and mTOR signaling in mammals. High-resolution cryoEM of porcine kidney V-ATPase with recombinant mEAK-7 showed that mEAK-7's TLDc domain interacts with V-ATPase's stator, whereas its C-terminal α helix binds V-ATPase's rotor. This crosslink would be expected to inhibit rotary catalysis. However, unlike the yeast TLDc protein Oxr1p, exogenous mEAK-7 does not inhibit V-ATPase and mEAK-7 overexpression in cells does not alter lysosomal or phagosomal pH. Instead, cryoEM suggests that the mEAK-7:V-ATPase interaction is disrupted by ATP-induced rotation of the rotor. Comparison of Oxr1p and mEAK-7 binding explains this difference. These results show that V-ATPase binding by TLDc domain proteins can lead to effects ranging from strong inhibition to formation of labile interactions that are sensitive to the enzyme's activity.
External linksLife Sci Alliance / PubMed:35794005 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.1 Å
Structure data

26385

7u8o

EMDB-26385, PDB-7u8o:
Structure of porcine V-ATPase with mEAK7 and SidK, Rotary state 2
Method: EM (single particle) / Resolution: 3.5 Å

26386

7u8p

EMDB-26386, PDB-7u8p:
Structure of porcine kidney V-ATPase with SidK, Rotary State 1
Method: EM (single particle) / Resolution: 3.7 Å

26387

7u8q

EMDB-26387, PDB-7u8q:
Structure of porcine kidney V-ATPase with SidK, Rotary State 2
Method: EM (single particle) / Resolution: 4.1 Å

26388

7u8r

EMDB-26388, PDB-7u8r:
Structure of porcine kidney V-ATPase with SidK, Rotary State 3
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • sus scrofa (pig)
  • legionella pneumophila (bacteria)
KeywordsMEMBRANE PROTEIN / proton translocation / complex / TLDc

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