TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains?

Trends Biochem Sci. 2002 Aug;27(8):381-3. doi: 10.1016/s0968-0004(02)02154-0.

Abstract

A family of membrane-associated proteins related to yeast Lag1p and mammalian TRAM has been identified. The family includes the protein product of CLN8, a gene mutated in progressive epilepsy with mental retardation. Mouse CLN8 is also mutated in the mnd/mnd mouse, a model for neuronal ceroid lipofuscinoses. The identification of these homologues has potential implications for our understanding of ceramide synthesis, lipid regulation and protein translocation in the endoplasmic reticulum.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Humans
  • Lipid Metabolism*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Membrane Transport Proteins
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid

Substances

  • CLN8 protein, human
  • Cln8 protein, mouse
  • Fungal Proteins
  • LAG1 protein, S cerevisiae
  • Membrane Glycoproteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • TRAM1 protein, human
  • translocating chain-associating membrane protein (TRAM)