Over 50 years ago the lupus erythematosus (LE) cell phenomenon was described and 
this was quickly followed by the introduction of the LE cell test and indirect 
immunofluorescence (IIF) to detect antinuclear antibodies (ANA) in clinical 
laboratories. Recently, attention has turned to the identification of the 
autoantigens that bind to cytoplasmic organelles such as the Golgi complex, 
endosomes and other "cytoplasmic somes". Three endosome autoantigens include 
early endosome antigen 1 (EEA1, 160 kDa), cytoplasmic linker protein-170 
(CLIP-170, 170 kDa), and lysobisphosphatidic acid (LBPA). Antibodies to EEA1 
were seen in a variety of conditions but approximately 40% of the patients had a 
neurological disease. Despite the prominence of lysosomes in cells and tissues, 
reports of autoantibodies are limited to the lysosomal antigen h-LAMP-2 and the 
cytoplasmic antineutrophil antibodies (cANCA). Autoantigens in the Golgi complex 
include giantin/macrogolgin, golgin-245, golgin 160, golgin-97, golgin 95/gm130, 
and golgin-67. More recently, there has been an interest in autoantibodies that 
bind components of the "SMN complex" or the "assemblyosome". Arginine/glycine 
(RG)-rich domains in components of the SMN complex interact with Sm, like-Sm 
(LSm), fibrillarin, RNA helicase A (Gu), and coilin proteins, all of which are 
antigen targets in a variety of diseases. More recently, components of a novel 
cytoplasmic structure named GW bodies (GWBs) have been identified as targets of 
human autoantibodies. Components of GWBs include GW182, a unique mRNA-binding 
protein, like Sm proteins (LSms), and decapping (hDcp1) and exonuclease (Xrn) 
enzymes. Current evidence suggests that GWBs are involved in the cytoplasmic 
processing of mRNAs. Autoantibodies to the "cytoplasmic somes" are relatively 
uncommon and serological tests to detect most of them are not widely available.