PMID- 10660298
OWN - NLM
STAT- MEDLINE
DCOM- 20000320
LR  - 20211203
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 10
IP  - 1
DP  - 2000 Jan 13
TI  - Cactus-independent regulation of Dorsal nuclear import by the ventral signal.
PG  - 23-6
AB  - Rel-family transcription factors function in a variety of biological processes,
      including development and immunity. During early Drosophila development, the
      Toll-Cactus-Dorsal pathway regulates the establishment of the embryonic
      dorsoventral axis. The last step in this pathway is the graded nuclear import of 
      the Rel protein Dorsal. Dorsal is retained in the cytoplasm by the IkappaB-family
      protein Cactus. Phosphorylation of both Dorsal and Cactus is regulated by a
      Toll-receptor-dependent ventral signal relayed by the Tube and Pelle proteins.
      Phosphorylation of Cactus leads to its degradation and to the release of Dorsal
      to form a ventral-to-dorsal nuclear Dorsal gradient. To understand how the
      ventral signal regulates the nuclear import and activity of Dorsal, we deleted
      its conserved nuclear localization signal (NLS). The truncated protein remained
      in the cytoplasm and could antagonize the function of wild-type Dorsal,
      suggesting that Dorsal forms a dimer in the cytoplasm. Further, the nuclear
      import of a mutant Dorsal protein that failed to interact with Cactus was still
      regulated by the ventral signal. Our results are consistent with a model in which
      ventral signal-dependent modification of both Cactus and Dorsal is required for
      the graded nuclear import of Dorsal.
FAU - Drier, E A
AU  - Drier EA
AD  - Waksman Institute, Department of Molecular Biology and Biochemistry, Rutgers
      University, Piscataway, New Jersey 08854-8020, USA.
FAU - Govind, S
AU  - Govind S
FAU - Steward, R
AU  - Steward R
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  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Insect Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Tl protein, Drosophila)
RN  - 0 (Toll-Like Receptors)
RN  - 0 (Transcription Factors)
RN  - 0 (dl protein, Drosophila)
RN  - 0 (tub protein, Drosophila)
RN  - 149059-01-8 (cact protein, Drosophila)
RN  - EC 2.7.1.- (pll protein, Drosophila)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
SB  - IM
MH  - Animals
MH  - Animals, Genetically Modified
MH  - DNA-Binding Proteins/genetics/physiology
MH  - Dimerization
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster/*embryology/genetics
MH  - Embryo, Nonmammalian/physiology/ultrastructure
MH  - Insect Proteins/genetics/physiology
MH  - Membrane Glycoproteins/genetics/physiology
MH  - Morphogenesis/genetics
MH  - Nuclear Proteins/genetics/physiology
MH  - Phenotype
MH  - Phosphoproteins/genetics/physiology
MH  - Phosphorylation
MH  - Protein Processing, Post-Translational
MH  - Protein Serine-Threonine Kinases/genetics/physiology
MH  - *Receptors, Cell Surface
MH  - Toll-Like Receptors
MH  - *Transcription Factors
EDAT- 2000/02/05 09:00
MHDA- 2000/03/25 09:00
CRDT- 2000/02/05 09:00
PHST- 2000/02/05 09:00 [pubmed]
PHST- 2000/03/25 09:00 [medline]
PHST- 2000/02/05 09:00 [entrez]
AID - S0960-9822(99)00267-5 [pii]
AID - 10.1016/s0960-9822(99)00267-5 [doi]
PST - ppublish
SO  - Curr Biol. 2000 Jan 13;10(1):23-6. doi: 10.1016/s0960-9822(99)00267-5.