Presence of a voltage-dependent anion channel 1 in the rat postsynaptic density fraction.
Little is known about the molecular organization and functions of the postsynaptic density (PSD), a cytoskeletal specialization on the postsynaptic membrane. In an attempt to elucidate the protein composition of PSD, we have sequenced a 35 kDa protein of the rat forebrain PSD fraction. Amino acid sequence information of the tryptic peptides and immunoblot analyses revealed that the protein is a voltage-dependent anion channel 1 (VDAC1). VDAC1 was enriched in the PSD fraction and was partially soluble in 1% n-octyl glucoside (NOG) or Triton X-100. Our data indicate that VDAC1, which is originally found in the outer mitochondrial membrane, is also present in the central nervous system (CNS) synapses in association with the PSD 'core'.
Moon
J I
JI
Department of Microbiology, College of Natural Sciences, Kyungpook National University, Taegu, Korea.
Jung
Y W
YW
Ko
B H
BH
De Pinto
V
V
Jin
I
I
Moon
I S
IS
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D015151:Immunoblotting; D018272:Porins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D012995:Solubility; D013347:Subcellular Fractions / Q000378:metabolism*; D013569:Synapses / Q000378:metabolism* / Q000648:ultrastructure; D050995:Voltage-Dependent Anion Channel 1; D050994:Voltage-Dependent Anion Channels
D018272:Porins; C494764:Vdac1 protein, rat; D050994:Voltage-Dependent Anion Channels; D050995:Voltage-Dependent Anion Channel 1