PMID- 10524200
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1446
IP  - 3
DP  - 1999 Sep 3
TI  - Human phosducin-like protein (hPhLP) messenger RNA stability is regulated by
      cis-acting instability elements present in the 3'-untranslated region.
PG  - 253-64
AB  - Phosducin (Pd) and phosducin-like protein (PhLP) have been shown to regulate
      G-protein signaling by binding G beta gamma subunits. To better define the
      function and regulation of PhLP, and to begin to investigate its potential role
      in human pathophysiological states, we have cloned the human PhLP (hPhLP) cDNA.
      The hPhLP shows 92% identity with the rat PhLP (rPhLP). However, unlike the
      rPhLP, no evidence of hPhLP isoforms were detected in the human tissues
      investigated. Additionally, unlike the rPhLP, alternative polyadenylation sites
      were detected in hPhLP cDNA clones which corresponded with two distinct mRNA
      transcripts, 1.2 kb and 3.1 kb, respectively. Interestingly, the predominantly
      expressed long transcript contains multiple AU-rich elements (AREs) in its
      3'-untranslated region (3'-UTR) which have been shown to correlate with rapid
      mRNA turnover and translational control. This study shows that the hPhLP AREs are
      functional both in vitro and in vivo, with the long transcript exhibiting a much 
      shorter mRNA half-life. We also demonstrate that subcloning of either the
      full-length 3'-UTR or the ARE-rich region of the long transcript immediately
      following the stop codon of luciferase reporter gene confers instability to the
      luciferase mRNA and results in a ninefold reduction of luciferase activity in the
      cell types investigated. Taken together, these findings suggest that the AREs
      present in the long hPhLP mRNA may play a critical role in the regulation of
      hPhLP gene expression.
FAU - Lazarov, M E
AU  - Lazarov ME
AD  - Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT
      84602, USA.
FAU - Martin, M M
AU  - Martin MM
FAU - Willardson, B M
AU  - Willardson BM
FAU - Elton, T S
AU  - Elton TS
LA  - eng
GR  - R01 EY012287/EY/NEI NIH HHS/United States
GR  - HL48848/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Extracts)
RN  - 0 (DNA, Complementary)
RN  - 0 (G-protein Beta gamma)
RN  - 0 (GTP-Binding Protein beta Subunits)
RN  - 0 (GTP-Binding Protein gamma Subunits)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (PDCL protein, human)
RN  - 0 (RNA, Messenger)
RN  - 1CC1JFE158 (Dactinomycin)
RN  - EC 1.13.12.- (Luciferases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Carrier Proteins/chemistry/*genetics/metabolism
MH  - Cell Extracts/chemistry
MH  - DNA, Complementary/isolation & purification
MH  - Dactinomycin
MH  - *GTP-Binding Protein beta Subunits
MH  - *GTP-Binding Protein gamma Subunits
MH  - GTP-Binding Proteins/antagonists & inhibitors/metabolism
MH  - Gene Expression Regulation
MH  - Gene Library
MH  - Half-Life
MH  - *Heterotrimeric GTP-Binding Proteins
MH  - Humans
MH  - Luciferases/genetics
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/chemistry/*genetics/metabolism
MH  - RNA, Messenger/*chemistry/isolation & purification
MH  - Regression Analysis
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
AID - S0167-4781(99)00098-6 [pii]
AID - 10.1016/s0167-4781(99)00098-6 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Sep 3;1446(3):253-64. doi:
      10.1016/s0167-4781(99)00098-6.