PMID- 10323867
OWN - NLM
STAT- MEDLINE
DCOM- 19990604
LR  - 20211203
IS  - 0890-9369 (Print)
IS  - 0890-9369 (Linking)
VI  - 13
IP  - 9
DP  - 1999 May 1
TI  - The Drosophila Pkn protein kinase is a Rho/Rac effector target required for 
      dorsal closure during embryogenesis.
PG  - 1168-80
AB  - The PKN family of PKC-related protein kinases constitutes the major Rho 
      GTPase-associated protein kinase activities detected in mammalian tissues. 
      However, the biological functions of these kinases are unknown. We have 
      identified a closely related PKN homolog in Drosophila (Pkn) that binds 
      specifically to GTP-activated Rho1 and Rac1 GTPases through distinct binding 
      sites on Pkn. The interaction of Pkn with either of these GTPases results in 
      increased kinase activity, suggesting that Pkn is a shared Rho/Rac effector 
      target. Characterization of a loss-of-function mutant of Drosophila Pkn revealed 
      that this kinase is required specifically for the epidermal cell shape changes 
      during the morphogenetic process of dorsal closure of the developing embryo. 
      Moreover, Pkn, as well as the Rho1 GTPase, mediate a pathway for cell shape 
      changes in dorsal closure that is independent of the previously reported Rac 
      GTPase-mediated Jun amino (N)-terminal kinase (JNK) cascade that regulates gene 
      expression required for dorsal closure. Thus, it appears that distinct but 
      coordinated Rho- and Rac-mediated signaling pathways regulate the cell shape 
      changes required for dorsal closure and that Pkn provides a GTPase effector 
      function for cell shape changes in vivo, which acts together with a Rac-JNK 
      transcriptional pathway in the morphogenesis of the Drosophila embryo.
FAU - Lu, Y
AU  - Lu Y
AD  - Massachusetts General Hospital Cancer Center and Harvard Medical School, 
      Charlestown, Massachusetts 02129, USA.
FAU - Settleman, J
AU  - Settleman J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Genes Dev
JT  - Genes & development
JID - 8711660
RN  - 0 (DNA Primers)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Insect Proteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (Rho1 protein, Drosophila)
RN  - EC 3.6.5.2 (rac GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rho GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Body Patterning/genetics
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Cell Size
MH  - Cloning, Molecular
MH  - DNA Primers/genetics
MH  - Drosophila/*embryology/*enzymology/genetics
MH  - Drosophila Proteins
MH  - GTP-Binding Proteins/*metabolism
MH  - Genes, Insect
MH  - Insect Proteins/*metabolism
MH  - JNK Mitogen-Activated Protein Kinases
MH  - *Mitogen-Activated Protein Kinases
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Serine-Threonine Kinases/chemistry/genetics/*metabolism
MH  - Protein-Tyrosine Kinases/chemistry/genetics/*metabolism
MH  - Signal Transduction
MH  - rac GTP-Binding Proteins
MH  - *rho GTP-Binding Proteins
PMC - PMC316938
EDAT- 1999/05/14 00:00
MHDA- 1999/05/14 00:01
CRDT- 1999/05/14 00:00
PHST- 1999/05/14 00:00 [pubmed]
PHST- 1999/05/14 00:01 [medline]
PHST- 1999/05/14 00:00 [entrez]
AID - 10.1101/gad.13.9.1168 [doi]
PST - ppublish
SO  - Genes Dev. 1999 May 1;13(9):1168-80. doi: 10.1101/gad.13.9.1168.