Porin interaction with hexokinase and glycerol kinase: Metabolic microcompartmentation at the outer mitochondrial membrane

Volker Adams, Lisa Griffin, Jeffrey Towbin, Bruce Gelb, Kim Worley, Edward R.B. McCabe

Research output: Contribution to journalReview article

131 Citations (Scopus)

Abstract

Porin is the pore-forming protein involved in the movement of adenine nucleotides across the outer mitochondrial membrane (OMM). Hexokinase and glycerol kinase interact with porin on the outer surface of the OMM in a manner which provides these enzymes with preferred access to the ATP generated in the mitochondrion. We review recent evidence which permits refinement of our knowledge of these proteins and their interactions at the OMM. The involvement of this system in metabolic microcompartmentation is discussed, as well as possible pathological consequences of its disruption in malignancy and genetic deficiences of hexokinase, glycerol kinase, and porin.

Original languageEnglish (US)
Pages (from-to)271-291
Number of pages21
JournalBiochemical Medicine and Metabolic Biology
Volume45
Issue number3
DOIs
StatePublished - Jan 1 1991

Fingerprint

Glycerol Kinase
Porins
Hexokinase
Mitochondrial Membranes
Membranes
Mitochondria
Adenine Nucleotides
Proteins
Adenosine Triphosphate
Enzymes
Neoplasms

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry

Cite this

Porin interaction with hexokinase and glycerol kinase : Metabolic microcompartmentation at the outer mitochondrial membrane. / Adams, Volker; Griffin, Lisa; Towbin, Jeffrey; Gelb, Bruce; Worley, Kim; McCabe, Edward R.B.

In: Biochemical Medicine and Metabolic Biology, Vol. 45, No. 3, 01.01.1991, p. 271-291.

Research output: Contribution to journalReview article

Adams, Volker ; Griffin, Lisa ; Towbin, Jeffrey ; Gelb, Bruce ; Worley, Kim ; McCabe, Edward R.B. / Porin interaction with hexokinase and glycerol kinase : Metabolic microcompartmentation at the outer mitochondrial membrane. In: Biochemical Medicine and Metabolic Biology. 1991 ; Vol. 45, No. 3. pp. 271-291.
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