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Identification and characterization of a new phospholipase C-like protein, PLC-L(2).
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1999 Dec 09; Vol. 266 (1), pp. 97-103. - Publication Year :
- 1999
-
Abstract
- We have isolated a cDNA encoding a novel protein, PLC-L(2), with homology to the phospholipase C-like protein PLC-L and delta-type phospholipase C. PLC-L(2) contains a relatively well-conserved PH domain, PLC catalytic region, and X and Y domains. However, it did not have PLC activity. This inactivation was thought to be caused by the replacement of two amino acids that are essential for PLC activity, His356 and Tyr552, with Thr and Phe in the X and Y domain. PLC-L(2) has a wide distribution with strong expression in skeletal muscle and mapped to chromosome 3p24-25. The PH domain of PLC-L(2) bound strongly to PI(4,5)P(2) and Ins(1,4,5)P(3), and moderately to PI(4)P and PI(3,4,5)P(3). PLC-L(2) predominantly localized to perinuclear areas in both myoblast and myotube C2C12 cells. Ectopically expressed GFP-PLC-L(2) also mainly localized in perinuclear areas, including endoplasmic reticulum in COS 7 cells. Furthermore, the expression of GFP-PH showed the same intracellular distribution as the full-length PLC-L(2). All these results suggest that PLC-L(2) plays an important role in the regulation of Ins(1,4, 5)P(3) around the endoplasmic reticulum on which the Ins(1,4,5)P(3) receptor exists.<br /> (Copyright 1999 Academic Press.)
- Subjects :
- Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Binding, Competitive
Catalytic Domain
Cell Line
Cell Membrane chemistry
Chromosomes, Human, Pair 3 genetics
Cloning, Molecular
Cytoplasm chemistry
Endoplasmic Reticulum chemistry
Humans
Inositol 1,4,5-Trisphosphate metabolism
Intracellular Signaling Peptides and Proteins
Isoenzymes chemistry
Isoenzymes metabolism
Mice
Molecular Sequence Data
Muscle, Skeletal chemistry
Muscle, Skeletal cytology
Phosphatidylinositol 4,5-Diphosphate metabolism
Phospholipases chemistry
Physical Chromosome Mapping
RNA, Messenger analysis
RNA, Messenger genetics
Sequence Homology, Amino Acid
Type C Phospholipases metabolism
Phospholipases genetics
Phospholipases metabolism
Type C Phospholipases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 266
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 10581172
- Full Text :
- https://doi.org/10.1006/bbrc.1999.1784