PMID- 14745013
OWN - NLM
STAT- MEDLINE
DCOM- 20040409
LR  - 20190108
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 101
IP  - 6
DP  - 2004 Feb 10
TI  - The Drosophila gene Start1: a putative cholesterol transporter and key regulator 
      of ecdysteroid synthesis.
PG  - 1601-6
AB  - Human metastatic lymph node 64 (MLN64) is a transmembrane protein that shares 
      homology with the cholesterol-binding vertebrate steroid acute regulatory protein 
      (StAR)-related lipid transfer domain (START) and is involved in cholesterol 
      traffic and steroid synthesis. We identified a Drosophila melanogaster gene whose 
      putative protein product shows extensive homology with MLN64 and that we name 
      Start1 (FlyBase CG3522). The putative Start1 protein, derived from Start1 cDNA 
      sequences, contains an additional 122 aa of unknown function within the 
      StAR-related lipid transfer domain. Similar inserts seem to exist in the Start1 
      homologues of Drosophila pseudoobscura and Anopheles gambiae, but not in the 
      homologous protein of the urochordate Ciona intestinalis. Immunostaining using an 
      insert-specific antibody confirms the presence of the insert in the cytoplasm. 
      Whereas RT-PCR data indicate that Start1 is expressed ubiquitously, RNA in situ 
      hybridizations demonstrate its overexpression in prothoracic gland cells, where 
      ecdysteroids are synthesized from cholesterol. Transcripts of Start1 are 
      detectable in embryonic ring gland progenitor cells and are abundant in 
      prothoracic glands of larvae showing wave-like expression during larval stages. 
      In adults, Start1 is expressed in nurse cells of the ovary. These observations 
      are consistent with the assumption that Start1 plays a key role in the regulation 
      of ecdysteroid synthesis. Vice versa, the expression of Start1 itself seems to 
      depend on ecdysone, as in the ecdysone-deficient mutant ecd-1, Start1 expression 
      is severely reduced.
FAU - Roth, Guenther E
AU  - Roth GE
AD  - Institut fur Biologie, Freie Universitat Berlin, Arnimallee 7, 14195 Berlin, 
      Germany. groth@genetik.fu-berlin.de
FAU - Gierl, Mathias S
AU  - Gierl MS
FAU - Vollborn, Lars
AU  - Vollborn L
FAU - Meise, Martin
AU  - Meise M
FAU - Lintermann, Ruth
AU  - Lintermann R
FAU - Korge, Guenter
AU  - Korge G
LA  - eng
SI  - GENBANK/AY455866
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20040126
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Drosophila Proteins)
RN  - 0 (Ecdysteroids)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Start1 protein, Drosophila)
RN  - 3604-87-3 (Ecdysone)
RN  - 97C5T2UQ7J (Cholesterol)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Biological Transport
MH  - Cholesterol/*metabolism
MH  - Cloning, Molecular
MH  - Drosophila Proteins/chemistry/*genetics/metabolism
MH  - Drosophila melanogaster/*genetics
MH  - Ecdysone/physiology
MH  - Ecdysteroids/*biosynthesis
MH  - Gene Expression Regulation/physiology
MH  - In Situ Hybridization
MH  - Membrane Transport Proteins/chemistry/*genetics/metabolism
MH  - Molecular Sequence Data
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sequence Homology, Amino Acid
PMC - PMC341787
EDAT- 2004/01/28 05:00
MHDA- 2004/04/10 05:00
PMCR- 2004/08/10
CRDT- 2004/01/28 05:00
PHST- 2004/01/28 05:00 [pubmed]
PHST- 2004/04/10 05:00 [medline]
PHST- 2004/01/28 05:00 [entrez]
PHST- 2004/08/10 00:00 [pmc-release]
AID - 0308212100 [pii]
AID - 1011601 [pii]
AID - 10.1073/pnas.0308212100 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1601-6. doi: 
      10.1073/pnas.0308212100. Epub 2004 Jan 26.