PMID- 10652308
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - Similarities in function and gene structure of cytohesin-4 and cytohesin-1,
      guanine nucleotide-exchange proteins for ADP-ribosylation factors.
PG  - 3221-30
AB  - Activation of ADP-ribosylation factors (ARFs), approximately 20-kDa GTPases that 
      are inactive in the GDP-bound form, depends on guanine nucleotide-exchange
      proteins (GEPs) to accelerate GTP binding. A novel ARF GEP, designated
      cytohesin-4, was cloned from a human brain cDNA library. Deduced amino acid
      sequence of the 47-kDa protein contains the same structural components present in
      cytohesin -1, -2, and -3, including an approximately 200-amino acid Sec7 domain
      with an approximately 100-residue pleckstrin homology domain near the C terminus.
      The Sec7 domain sequence is 77% identical to those of other cytohesins.
      Structures of the cytohesin-4 and cytohesin-1 genes were remarkably similar,
      except for an extra 3-base pair (GAG) exon present in cytohesin-1. Two mRNAs with
      and without the 3-base pair sequence were found in brain in different ratios for 
      cytohesin-1, -2, and -3 but not cytohesin-4. Recombinant cytohesin-4 stimulated
      guanosine 5'-3-O-(thio)triphosphate binding by human ARF1 and ARF5 but not ARF6. 
      Like other cytohesins and unlike the approximately 200-kDa ARF GEPs, it was not
      inhibited by brefeldin A. A cytohesin-4 mRNA of approximately 3.7 kilobases,
      abundant in leukocytes, was not detected in most tissues. Among separated
      populations of blood cells, approximately 90% of CD33(+) (monocytes), 80% of
      CD2(+) (NK/T), and 10-20% of CD19(+) (B) cells contained cytohesin-4 mRNA by in
      situ hybridization. Thus, in gene structure and brefeldin A-insensitive GEP
      activity, cytohesin-4 resembles other cytohesins, but its tissue distribution
      differs considerably, consistent with a different specific function.
FAU - Ogasawara, M
AU  - Ogasawara M
AD  - Pulmonary-Critical Care Medicine Branch, NHLBI, National Institutes of Health,
      Bethesda, Maryland 20892-1434, USA. ogawawam@gwgate.nhlbi.nih.gov
FAU - Kim, S C
AU  - Kim SC
FAU - Adamik, R
AU  - Adamik R
FAU - Togawa, A
AU  - Togawa A
FAU - Ferrans, V J
AU  - Ferrans VJ
FAU - Takeda, K
AU  - Takeda K
FAU - Kirby, M
AU  - Kirby M
FAU - Moss, J
AU  - Moss J
FAU - Vaughan, M
AU  - Vaughan M
LA  - eng
SI  - GENBANK/AF125346
SI  - GENBANK/AF125362
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CYTH4 protein, human)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DNA, Complementary)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (Recombinant Proteins)
RN  - 0 (cytohesin-1)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factors)
SB  - IM
MH  - ADP-Ribosylation Factors/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Adhesion Molecules/*genetics/*metabolism
MH  - Cell Line
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics/isolation & purification
MH  - Guanine Nucleotide Exchange Factors/*genetics/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/genetics/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis
EDAT- 2000/02/01 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3221 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3221-30. doi: 10.1074/jbc.275.5.3221.