PMID- 10531358
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 44
DP  - 1999 Oct 29
TI  - Cloning and characterization of a novel human phosphatidylinositol transfer
      protein, rdgBbeta.
PG  - 31553-8
AB  - The various PITP, retinal degeneration B (rdgB), and amino-terminal domain
      interacting receptor (Nir) phosphatidylinositol transfer proteins can be divided 
      into two structural families. The small, soluble PITP isoforms contain only a
      phosphatidylinositol transfer domain and have been implicated in phosphoinositide
      signaling and vesicle trafficking. In contrast, the rdgB proteins, which include 
      Nir2 and Nir3, contain an amino-terminal PITP-like domain, an acidic,
      Ca(2+)-binding domain, six putative transmembrane domains, and a conserved
      carboxyl-terminal domain. However, the biological function of rdgB proteins is
      unclear. Here, we report the isolation of a cDNA encoding a novel rdgB protein,
      mammalian rdgBbeta (MrdgBbeta). The 38-kDa MrdgBbeta protein contains an
      amino-terminal PITP-like domain and a short carboxyl-terminal domain. In contrast
      to other rdgB-like proteins, MrdgBbeta contains no transmembrane motifs or the
      conserved carboxyl-terminal domain. Using Northern and reverse
      transcription-polymerase chain reaction analysis, we demonstrate that MrdgBbeta
      mRNA is ubiquitously expressed. Immunofluorescence analysis of ectopic MrdgBbeta 
      showed cytoplasmic staining, and the ability of recombinant MrdgBbeta to transfer
      phosphatidylinositol in vitro was similar to other PITP-like domains. Although
      early reports found functional degeneracy in vitro, the identification of a fifth
      mammalian PITP-like protein with a unique domain organization and widespread
      expression supports more recent results that suggest that different PITP-like
      domains have distinct functions in vivo.
FAU - Fullwood, Y
AU  - Fullwood Y
AD  - Ludwig Institute for Cancer Research, Courtauld Building, 91 Riding House St.,
      London W1P 8BT, United Kingdom.
FAU - dos Santos, M
AU  - dos Santos M
FAU - Hsuan, J J
AU  - Hsuan JJ
LA  - eng
SI  - GENBANK/AF171102
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (PITPNC1 protein, human)
RN  - 0 (Phosphatidylinositols)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Carrier Proteins/genetics/*metabolism
MH  - Cell Compartmentation
MH  - Cloning, Molecular
MH  - Cytoplasm/chemistry
MH  - Evolution, Molecular
MH  - Humans
MH  - *Membrane Proteins
MH  - Membrane Transport Proteins
MH  - Molecular Sequence Data
MH  - Phosphatidylinositols/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1074/jbc.274.44.31553 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 29;274(44):31553-8. doi: 10.1074/jbc.274.44.31553.