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Compositional complexity of rods and rings.

Cara R Schiavon1, Maxwell E Griffin1, Marinella Pirozzi2

  • 1Cancer Biology Graduate Program, Graduate Division of Biomedical and Biological Sciences, Laney Graduate School, Atlanta, GA 30307.

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Summary
This summary is machine-generated.

Rods and rings, structures formed by IMPDH, are more complex than previously thought. Their function involves regulatory GTPase ARL2 and endoplasmic reticulum proteins, with formation dependent on guanine nucleotide synthesis.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Rods and rings (RRs) are large cellular structures, often polymers of inosine monophosphate dehydrogenase (IMPDH).
  • Their role in regulating de novo guanine nucleotide synthesis is suggested but poorly understood.
  • RR formation can be induced by IMPDH inhibitors.

Purpose of the Study:

  • To investigate the molecular composition and regulation of rods and rings (RRs).
  • To identify novel inducers and disassemblers of RR formation.
  • To elucidate the maturation process and potential functions of RRs.

Main Methods:

  • Cellular localization studies to identify proteins within RRs.
  • Induction of RR formation using AICAR and glucose deprivation.
  • Disassembly experiments based on guanine nucleotide salvage pathways.

Main Results:

  • The regulatory GTPase ARL2, its binding partners, and endoplasmic reticulum proteins localize to RRs.
  • AICAR and glucose deprivation were identified as new inducers of RR formation.
  • RR disassembly occurs when guanine nucleotides are supplied via salvage synthesis.
  • RR maturation involves an ordered addition of IMPDH, ARL2, and ER proteins like calnexin.

Conclusions:

  • Rods and rings are complex structures involving IMPDH, ARL2, and ER proteins.
  • RR formation and disassembly are linked to guanine nucleotide synthesis and salvage pathways.
  • These findings suggest RRs may play roles in regulating nucleotide synthesis and interacting with intracellular membranes.