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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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A cytosolic, G alpha(q)- and beta gamma-insensitive splice variant of phospholipase C-beta 4

Cited 29 times inthomson ciCited 26 times inthomson ci
Title
A cytosolic, G alpha(q)- and beta gamma-insensitive splice variant of phospholipase C-beta 4
Author
Kim, MJMin, DSRyu, SHSuh, Pann-Ghill
Keywords
PROTEIN ALPHA-SUBUNIT; DROSOPHILA-MELANOGASTER; INOSITOL TRISPHOSPHATE; BOVINE CEREBELLUM; HUMAN PLATELETS; GROWTH-FACTOR; NORPA GENE; C ISOZYME; ACTIVATION; PURIFICATION
Issue Date
199802
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.273, no.6, pp.3618 - 3624
Abstract
Phospholipase C (PLC)-β4 has been considered to be a mammalian homolog of the NorpA PLC, which is responsible for visual signal transduction in Drosophila. We reported previously the cloning of a cDNA encoding rat phospholipase C-β4 (PLC-β4) (Kim, M.J., Bahk, Y.Y., Min, D. S., Lee, S.J., Ryu, S.H., and Suh, P.-G. (1993) Biochem. Biophys. Res. Commun. 194, 706- 712). We re- port now the isolation and characterization of a splice variant (PLC-β4b). PLC-β4b is identical to the 130-kDa PLC-β4 (PLC-β4a) except that the carboxyl-terminal 162 amino acids of PLC-β4a are replaced by 10 distinct amino acids. The existence of PLC-β4b transcripts in the rat brain was demonstrated by reverse transcription-polymerase chain reaction analysis. Immunological analysis using polyclonal antibody specific for PLC-β4b revealed that this splice variant exists in rat brain cytosol. To investigate functional differences between the two forms of PLC-β4, transient expression studies in COS-7 cells were conducted. We found that PLC-β4a was localized mainly in the particulate fraction of the cell, and it could be activated by Gα(q), whereas PLC-β4b was localized exclusively in the soluble fraction, and it could not be activated by Gα(q). In addition, both PLC-β4a and PLC- β4b were not activated by G-protein βγ-subunits purified from rat brain. These results suggest that PLC-β4b may be regulated by a mechanism different from that of PLC-β4a, and therefore it may play a distinct role in PLC- mediated signal transduction.
URI
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DOI
http://dx.doi.org/10.1074/jbc.273.6.3618
ISSN
0021-9258
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