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hnRNPs H, H′ and F behave differently with respect to posttranslational cleavage and subcellular localization
Author(s) -
Honoré Bent,
Vorum Henrik,
Baandrup Ulrik
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00911-4
Subject(s) - cytoplasm , heterogeneous nuclear ribonucleoprotein , subfamily , cleavage (geology) , nucleus , cell nucleus , subcellular localization , intracellular , nuclear localization sequence , microbiology and biotechnology , biology , nuclear export signal , nuclear protein , chemistry , biochemistry , rna , gene , ribonucleoprotein , transcription factor , paleontology , fracture (geology)
hnRNPs H, H′ and F belong to a subfamily of the hnRNPs sharing a high degree of sequence identity. Eukaryotic expression and specific C‐terminal antibodies were used to demonstrate great variation in the intracellular fate of the proteins. hnRNPs H and H′ become posttranslational cleaved into C‐terminal 35 kDa proteins (H C , H′ C ) and possibly into N‐terminal 22 kDa proteins. No detectable cleavage was observed for hnRNP F. hnRNP H/H′ is almost exclusively localized to the nucleus of many cell types while hnRNP F varies from a predominant nuclear localization in some cells to a predominant cytoplasmic localization in other cells. The different fates may reflect differences in functional roles that so far only have included nuclear functions. The presence of significant quantities of hnRNP F in the cytoplasm of many cells indicates that it also may have a functional role here.