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Structure paper

TitleLight-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly.
Journal, issue, pagesJ Cell Biol, Vol. 223, Issue 4, Year 2024
Publish dateApr 1, 2024
AuthorsS John Calise / Audrey G O'Neill / Anika L Burrell / Miles S Dickinson / Josephine Molfino / Charlie Clarke / Joel Quispe / David Sokolov / Rubén M Buey / Justin M Kollman /
PubMed AbstractInosine monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in guanosine triphosphate (GTP) synthesis and assembles into filaments in cells, which desensitizes the enzyme to feedback ...Inosine monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in guanosine triphosphate (GTP) synthesis and assembles into filaments in cells, which desensitizes the enzyme to feedback inhibition and boosts nucleotide production. The vertebrate retina expresses two splice variants IMPDH1(546) and IMPDH1(595). In bovine retinas, residue S477 is preferentially phosphorylated in the dark, but the effects on IMPDH1 activity and regulation are unclear. Here, we generated phosphomimetic mutants to investigate structural and functional consequences of S477 phosphorylation. The S477D mutation resensitized both variants to GTP inhibition but only blocked assembly of IMPDH1(595) filaments. Cryo-EM structures of both variants showed that S477D specifically blocks assembly of a high-activity assembly interface, still allowing assembly of low-activity IMPDH1(546) filaments. Finally, we discovered that S477D exerts a dominant-negative effect in cells, preventing endogenous IMPDH filament assembly. By modulating the structure and higher-order assembly of IMPDH, S477 phosphorylation acts as a mechanism for downregulating retinal GTP synthesis in the dark when nucleotide turnover is decreased.
External linksJ Cell Biol / PubMed:38323936 / PubMed Central
MethodsEM (single particle)
Resolution2.1 - 3.3 Å
Structure data

41986

8u7m

EMDB-41986, PDB-8u7m:
Human retinal variant phosphomimetic IMPDH1(595)-S477D free octamer bound by GTP, ATP, IMP, and NAD+
Method: EM (single particle) / Resolution: 3.1 Å

41989

8u7q

EMDB-41989, PDB-8u7q:
Human retinal variant phosphomimetic IMPDH1(546)-S477D filament bound by GTP, ATP, IMP, and NAD+, octamer-centered
Method: EM (single particle) / Resolution: 3.3 Å

42012

8u7v

EMDB-42012, PDB-8u7v:
Human retinal variant phosphomimetic IMPDH1(546)-S477D filament bound by GTP, ATP, IMP, and NAD+, interface-centered
Method: EM (single particle) / Resolution: 3.3 Å

42026

8u8o

EMDB-42026, PDB-8u8o:
Human retinal variant phosphomimetic IMPDH1(546)-S477D filament bound by ATP, IMP, and NAD+, octamer-centered
Method: EM (single particle) / Resolution: 2.4 Å

42029

8u8y

EMDB-42029, PDB-8u8y:
Human retinal variant phosphomimetic IMPDH1(546)-S477D filament bound by ATP, IMP, and NAD+, interface-centered
Method: EM (single particle) / Resolution: 2.1 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-IMP:
INOSINIC ACID / Inosinic acid

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / dehydrogenase / nucleotide synthesis / cytosol / phosphomimetic / filament

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