title: The VAP protein family: from cellular functions to motor neuron disease.
abstract: The VAMP-associated proteins (VAPs) are highly conserved integral endoplasmic reticulum membrane proteins implicated in diverse cellular functions, including the regulation of lipid transport and homeostasis, membrane trafficking, neurotransmitter release, stabilization of presynaptic microtubules, and the unfolded protein response. Recently, a single missense mutation within the human VAP-B gene was identified in three forms of familial motor neuron disease. In this review, we integrate results from studies of yeast, fly and mammalian VAPs that provide insight into the structural features of these proteins, the network of VAP-interacting proteins, their possible physiological functions, and their involvement in motor neuron disease.
authors.affiliation: The Molecular Cell Biology Department, Weizmann Institute of Science, Rehovot 76100, Israel. sima.lev@weizmann.ac.il
authors.forename: Sima
authors.initials: S
authors.lastname: Lev
authors.forename: Daniel
authors.initials: D
authors.lastname: Ben Halevy
authors.forename: Diego
authors.initials: D
authors.lastname: Peretti
authors.forename: Nili
authors.initials: N
authors.lastname: Dahan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D004331:Drosophila melanogaster / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D008954:Models, Biological; D008969:Molecular Sequence Data; D009046:Motor Neurons / Q000378:metabolism*; D020125:Mutation, Missense; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D016615:Telomere / Q000648:ultrastructure; D033921:Vesicular Transport Proteins / Q000378:metabolism*
chemical_list: D008055:Lipids; D033921:Vesicular Transport Proteins