PMID- 9202123
OWN - NLM
STAT- MEDLINE
DCOM- 19970717
LR  - 20221227
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 387
IP  - 6636
DP  - 1997 Jun 26
TI  - Fringe modulates Notch-ligand interactions.
PG  - 908-12
AB  - The Notch family of transmembrane receptor proteins mediate developmental 
      cell-fate decisions, and mutations in mammalian Notch genes have been implicated 
      in leukaemia, breast cancer, stroke and dementia. During wing development in 
      Drosophila, the Notch receptor is activated along the border between dorsal and 
      ventral cells, leading to the specification of specialized cells that express 
      Wingless (Wg) and organize wing growth and patterning. Three genes, fringe (fng), 
      Serrate (Ser) and Delta (Dl), are involved in the cellular interactions leading 
      to Notch activation. Ser and Dl encode transmembrane ligands for Notch, whereas 
      fng encodes a pioneer protein. We have investigated the relationship between 
      these genes by a combination of expression and coexpression studies in the 
      Drosophila wing. We found that Ser and Dl maintain each other's expression by a 
      positive feedback loop. fng is expressed specifically by dorsal cells and 
      functions to position and restrict this feedback loop to the developing 
      dorsal-ventral boundary. This is achieved by fng through a cell-autonomous 
      mechanism that inhibits a cell's ability to respond to Serrate protein and 
      potentiates its ability to respond to Delta protein.
FAU - Panin, V M
AU  - Panin VM
AD  - Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, 
      The State University, Piscataway, New Jersey 08855, USA.
FAU - Papayannopoulos, V
AU  - Papayannopoulos V
FAU - Wilson, R
AU  - Wilson R
FAU - Irvine, K D
AU  - Irvine KD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Insect Proteins)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Jagged-1 Protein)
RN  - 0 (Ligands)
RN  - 0 (Membrane Proteins)
RN  - 0 (N protein, Drosophila)
RN  - 0 (Receptors, Notch)
RN  - 0 (Ser protein, Drosophila)
RN  - 0 (Serrate-Jagged Proteins)
RN  - 0 (delta protein)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.222 (fng protein, Drosophila)
SB  - IM
MH  - Animals
MH  - Animals, Genetically Modified
MH  - Calcium-Binding Proteins
MH  - Cells, Cultured
MH  - Drosophila
MH  - Drosophila Proteins
MH  - Gene Expression Regulation, Developmental
MH  - Insect Proteins/genetics/*physiology
MH  - Intercellular Signaling Peptides and Proteins
MH  - Intracellular Signaling Peptides and Proteins
MH  - Jagged-1 Protein
MH  - Ligands
MH  - Membrane Proteins/genetics/*physiology
MH  - *N-Acetylglucosaminyltransferases
MH  - Receptors, Notch
MH  - Serrate-Jagged Proteins
MH  - Signal Transduction
MH  - Wings, Animal/embryology
EDAT- 1997/06/26 00:00
MHDA- 2001/03/23 10:01
CRDT- 1997/06/26 00:00
PHST- 1997/06/26 00:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1997/06/26 00:00 [entrez]
AID - 10.1038/43191 [doi]
PST - ppublish
SO  - Nature. 1997 Jun 26;387(6636):908-12. doi: 10.1038/43191.