PMID- 10458911
OWN - NLM
STAT- MEDLINE
DCOM- 19990930
LR  - 20071114
IS  - 0888-7543 (Print)
IS  - 0888-7543 (Linking)
VI  - 60
IP  - 1
DP  - 1999 Aug 15
TI  - Isolation, characterization, and mapping of the mouse and human Fgd2 genes,
      faciogenital dysplasia (FGD1; Aarskog syndrome) gene homologues.
PG  - 57-66
AB  - FGD1 encodes a guanine nucleotide exchange factor (GEF) that specifically
      activates the Rho GTPase Cdc42. FGD1 gene mutations result in faciogenital
      dysplasia (FGDY, Aarskog syndrome), an X-linked developmental disorder that
      adversely affects the formation of multiple skeletal structures. Database
      searches show that the Caenorhabditis elegans genome contains an FGD1 homologue. 
      Since C. elegans genes often have multiple vertebrate homologues, we hypothesized
      the existence of multiple mammalian FGD1-related sequences. Here we report the
      use of degenerate PCR to isolate and characterize the mouse and human Fgd2 genes,
      new members of the FGD1 gene family. Fgd2 cDNA encodes a 727-amino-acid protein
      with a predicted mass of 82 kDa. Fgd2 and FGD1 share a high degree of sequence
      identity that spans >560 contiguous amino acid residues. Fgd2, like FGD1,
      contains adjacent RhoGEF and PH domains, a second carboxy-terminal PH domain, and
      a distinctive FYVE domain. Genomic PCR studies indicate some degree of conserved 
      gene structure between Fgd2 and FGD1. Fgd2 transcripts are present in several
      diverse tissues and during mouse embryogenesis, suggesting a role in embryonic
      development. Genetic linkage and radiation hybrid mapping data show that Fgd2 and
      the human FGD2 ortholog map to syntenic regions of murine chromosome 17 and human
      chromosome 6p21.2, respectively. The observation that all FGD1 gene family
      members contain equivalent signaling domains and a conserved structural
      organization strongly suggests that these signaling domains form a canonical core
      structure for members of the FGD1 family of RhoGEF proteins.
CI  - Copyright 1999 Academic Press.
FAU - Pasteris, N G
AU  - Pasteris NG
AD  - Department of Human Genetics, University of Michigan Medical Center, Ann Arbor,
      Michigan, 48109-0688, USA.
FAU - Gorski, J L
AU  - Gorski JL
LA  - eng
SI  - GENBANK/AF017368
GR  - HD34446/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Genomics
JT  - Genomics
JID - 8800135
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (FGD1 protein, human)
RN  - 0 (FGD2 protein, human)
RN  - 0 (Fgd1 protein, mouse)
RN  - 0 (Fgd2 protein, mouse)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (Proteins)
RN  - 0 (RNA, Messenger)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Abnormalities, Multiple/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Chromosome Mapping
MH  - Chromosomes/genetics
MH  - Chromosomes, Human, Pair 6/genetics
MH  - Cloning, Molecular
MH  - DNA Primers
MH  - DNA, Complementary/chemistry/*genetics/isolation & purification
MH  - Facial Bones/abnormalities/metabolism
MH  - GTP-Binding Proteins/*genetics
MH  - *Guanine Nucleotide Exchange Factors
MH  - Humans
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Muridae
MH  - Polymerase Chain Reaction
MH  - Proteins/*genetics
MH  - RNA, Messenger/genetics/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - Urogenital Abnormalities/genetics
EDAT- 1999/08/25 00:00
MHDA- 1999/08/25 00:01
CRDT- 1999/08/25 00:00
PHST- 1999/08/25 00:00 [pubmed]
PHST- 1999/08/25 00:01 [medline]
PHST- 1999/08/25 00:00 [entrez]
AID - 10.1006/geno.1999.5903 [doi]
AID - S0888-7543(99)95903-7 [pii]
PST - ppublish
SO  - Genomics. 1999 Aug 15;60(1):57-66. doi: 10.1006/geno.1999.5903.