PMID- 11688569
OWN - NLM
STAT- MEDLINE
DCOM- 20011204
LR  - 20220215
IS  - 0950-1991 (Print)
IS  - 0950-1991 (Linking)
VI  - 128
IP  - 16
DP  - 2001 Aug
TI  - The receptor-like tyrosine phosphatase lar is required for epithelial planar 
      polarity and for axis determination within drosophila ovarian follicles.
PG  - 3209-20
AB  - The follicle cell monolayer that encircles each developing Drosophila oocyte 
      contributes actively to egg development and patterning, and also represents a 
      model stem cell-derived epithelium. We have identified mutations in the 
      receptor-like transmembrane tyrosine phosphatase Lar that disorganize follicle 
      formation, block egg chamber elongation and disrupt Oskar localization, which is 
      an indicator of oocyte anterior-posterior polarity. Alterations in actin filament 
      organization correlate with these defects. Actin filaments in the basal follicle 
      cell domain normally become polarized during stage 6 around the 
      anterior-posterior axis defined by the polar cells, but mutations in Lar 
      frequently disrupt polar cell differentiation and actin polarization. Lar 
      function is only needed in somatic cells, and (for Oskar localization) its action 
      is autonomous to posterior follicle cells. Polarity signals may be laid down by 
      these cells within the extracellular matrix (ECM), possibly in the distribution 
      of the candidate Lar ligand Laminin A, and read out at the time Oskar is 
      localized in a Lar-dependent manner. Lar is not required autonomously to polarize 
      somatic cell actin during stages 6. We show that Lar acts somatically early in 
      oogenesis, during follicle formation, and postulate that it functions in 
      germarium intercyst cells that are required for polar cell specification and 
      differentiation. Our studies suggest that positional information can be stored 
      transiently in the ECM. A major function of Lar may be to transduce such signals.
FAU - Frydman, H M
AU  - Frydman HM
AD  - Howard Hughes Medical Institute, Department of Embryology, Carnegie Institution 
      of Washington, Baltimore, MD 21210, USA.
FAU - Spradling, A C
AU  - Spradling AC
LA  - eng
GR  - HHMI/Howard Hughes Medical Institute/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Development
JT  - Development (Cambridge, England)
JID - 8701744
RN  - 0 (Actins)
RN  - 0 (Laminin)
RN  - 0 (Receptors, Cell Surface)
RN  - 151186-83-3 (laminin A)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 4)
SB  - IM
MH  - Actins/metabolism
MH  - Alleles
MH  - Animals
MH  - Blotting, Northern
MH  - Body Patterning
MH  - Cell Differentiation
MH  - Drosophila
MH  - Epithelium/*embryology
MH  - Extracellular Matrix/metabolism
MH  - Female
MH  - In Situ Hybridization
MH  - Infertility, Female
MH  - Laminin/metabolism
MH  - Microscopy, Electron, Scanning
MH  - Microscopy, Fluorescence
MH  - Models, Anatomic
MH  - Models, Biological
MH  - Mutation
MH  - Ovarian Follicle/*embryology/metabolism
MH  - Ovary/*embryology
MH  - Protein Tyrosine Phosphatases/*metabolism/*physiology
MH  - Receptor-Like Protein Tyrosine Phosphatases, Class 4
MH  - *Receptors, Cell Surface
MH  - Signal Transduction
EDAT- 2001/11/02 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/11/02 10:00
PHST- 2001/11/02 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/11/02 10:00 [entrez]
AID - 10.1242/dev.128.16.3209 [doi]
PST - ppublish
SO  - Development. 2001 Aug;128(16):3209-20. doi: 10.1242/dev.128.16.3209.