A family of RS domain proteins with novel subcellular localization and trafficking.
We report the sequence, conservation and cell biology of a novel protein, Psc1, which is expressed and regulated within the embryonic pluripotent cell population of the mouse. The Psc1 sequence includes an RS domain and an RNA recognition motif (RRM), and a sequential arrangement of protein motifs that has not been demonstrated for other RS domain proteins. This arrangement was conserved in a second mouse protein (BAC34721). The identification of Psc1 and BAC34721 homologues in vertebrates and related proteins, more widely throughout evolution, defines a new family of RS domain proteins termed acidic rich RS (ARRS) domain proteins. Psc1 incorporated into the nuclear speckles, but demonstrated novel aspects of subcellular distribution including localization to speckles proximal to the nuclear periphery and localization to punctate structures in the cytoplasm termed cytospeckles. Integration of Psc1 into cytospeckles was dependent on the RRM. Cytospeckles were dynamic within the cytoplasm and appeared to traffic into the nucleus. These observations suggest a novel role in RNA metabolism for ARRS proteins.
Kavanagh
Steven J
SJ
School of Molecular and Biomedical Science, University of Adelaide Adelaide 5005, Australia.
Schulz
Thomas C
TC
Davey
Philippa
P
Claudianos
Charles
C
Russell
Carrie
C
Rathjen
Peter D
PD
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D022003:Cell Nucleus Structures / Q000737:chemistry; D002522:Chlorocebus aethiops; D017124:Conserved Sequence; D003593:Cytoplasm / Q000737:chemistry; D022083:Cytoplasmic Structures / Q000737:chemistry; D018076:DNA, Complementary / Q000737:chemistry / Q000302:isolation & purification; D019143:Evolution, Molecular; D051379:Mice; D008870:Microtubules / Q000378:metabolism; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism
D018076:DNA, Complementary; D009687:Nuclear Proteins; D011506:Proteins; D016601:RNA-Binding Proteins; C453239:Rbm27 protein, mouse
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