PMID- 10364432
OWN - NLM
STAT- MEDLINE
DCOM- 19990701
LR  - 20161019
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 210
IP  - 1
DP  - 1999 Jun 1
TI  - Nuclear entry of the Drosophila melanogaster nuclear lamina protein YA correlates
      with developmentally regulated changes in its phosphorylation state.
PG  - 124-34
AB  - The Drosophila melanogaster YA protein is a maternally provided nuclear lamina
      component that is essential during the transition from meiosis to mitosis at the 
      beginning of embryogenesis. Localization of YA to the nuclear envelope is
      required for its function; this localization is cell cycle-dependent during
      embryogenesis. Here we show that the ability of YA to enter nuclei is modulated
      during development. In developing egg chambers, YA protein is made but excluded
      from nuclei of nurse cells and oocytes; upon egg activation, YA acquires the
      ability to enter nuclei and becomes incorporated into the nuclear lamina in
      unfertilized eggs and embryos. This localization switch correlates with changes
      in the phosphorylation state of YA. YA in ovaries is hyperphosphorylated relative
      to YA in unfertilized eggs and embryos. Through site-directed mutagenesis, we
      identified 443T, a potential phosphorylation site for both cyclin-dependent
      protein kinase and mitogen-activated-protein kinase, as one of the sites likely
      involved in this developmental control. Our results suggest that phosphorylation 
      plays a role in modulating the localization of YA during development. A model for
      developmental regulation of the nuclear entry of YA is proposed and implications 
      for understanding Drosophila egg activation are discussed.
CI  - Copyright 1999 Academic Press.
FAU - Yu, J
AU  - Yu J
AD  - Section of Genetics and Development, Cornell University, Ithaca, New York,
      14853-2703, USA.
FAU - Liu, J
AU  - Liu J
FAU - Song, K
AU  - Song K
FAU - Turner, S G
AU  - Turner SG
FAU - Wolfner, M F
AU  - Wolfner MF
LA  - eng
GR  - R01 GM044659/GM/NIGMS NIH HHS/United States
GR  - GM07273/GM/NIGMS NIH HHS/United States
GR  - GM44659/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Chromosomal Proteins, Non-Histone)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 135315-84-3 (fs(1)Ya protein, Drosophila)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.22 (Cyclin-Dependent Kinases)
SB  - IM
MH  - Animals
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Cell Cycle
MH  - *Chromosomal Proteins, Non-Histone
MH  - Cyclin-Dependent Kinases/metabolism
MH  - *DNA-Binding Proteins
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster/*embryology/genetics
MH  - Fluorescent Antibody Technique
MH  - Glycosylation
MH  - Membrane Proteins/*metabolism
MH  - Nuclear Proteins/*metabolism
MH  - Ovum/metabolism
MH  - Phosphoproteins/analysis
MH  - Phosphorylation
MH  - Reproduction
EDAT- 1999/06/12 00:00
MHDA- 1999/06/12 00:01
CRDT- 1999/06/12 00:00
PHST- 1999/06/12 00:00 [pubmed]
PHST- 1999/06/12 00:01 [medline]
PHST- 1999/06/12 00:00 [entrez]
AID - S0012-1606(99)99264-3 [pii]
AID - 10.1006/dbio.1999.9264 [doi]
PST - ppublish
SO  - Dev Biol. 1999 Jun 1;210(1):124-34. doi: 10.1006/dbio.1999.9264.