PMID- 10375398
OWN - NLM
STAT- MEDLINE
DCOM- 19990715
LR  - 20131121
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 367
IP  - 1
DP  - 1999 Jul 1
TI  - Phosphorylation and glycosylation of nucleoporins.
PG  - 51-60
AB  - The nuclear pore complex mediates macromolecular transport between the nucleus
      and cytoplasm. Many nuclear pore components (nucleoporins) are modified by both
      phosphate and O-linked N-acetylglucosamine (O-GlcNAc). Among its many functions, 
      protein phosphorylation plays essential roles in cell cycle progression. The role
      of O-GlcNAc addition is unknown. Here, levels of nucleoporin phosphorylation and 
      glycosylation during cell cycle progression are examined. Whereas nuclear pore
      glycoproteins are phosphorylated in a cell-cycle-dependent manner, levels of
      O-GlcNAc remain constant. The major nucleoporin p62 can be phosphorylated in
      vitro by protein kinase A and glycogen synthase kinase (GSK)-3alpha but not by
      cyclin B/cdc2 or GSK-3beta. The consensus sites of these kinases resemble sites
      which can be glycosylated by O-GlcNAc transferase. These data are consistent with
      a model that O-GlcNAc limits nucleoporin hyperphosphorylation during M-phase and 
      hastens the resumption of regulated nuclear transport at the completion of cell
      division.
CI  - Copyright 1999 Academic Press.
FAU - Miller, M W
AU  - Miller MW
AD  - Department of Biological Sciences, Wright State University, Dayton, Ohio,
      45435-0001, USA. mwmiller@wright.edu
FAU - Caracciolo, M R
AU  - Caracciolo MR
FAU - Berlin, W K
AU  - Berlin WK
FAU - Hanover, J A
AU  - Hanover JA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphates)
RN  - 0 (Protein Isoforms)
RN  - 0 (Wheat Germ Agglutinins)
RN  - 0 (nuclear pore protein p62)
RN  - EC 2.7.11.- (Glycogen Synthase Kinases)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
RN  - EC 2.7.11.26 (Glycogen Synthase Kinase 3)
RN  - V956696549 (Acetylglucosamine)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Acetylglucosamine/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - CDC2 Protein Kinase/metabolism
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Cell Cycle
MH  - Cell Line
MH  - Cyclic AMP-Dependent Protein Kinases/metabolism
MH  - Galactose/metabolism
MH  - Glycogen Synthase Kinase 3
MH  - Glycogen Synthase Kinases
MH  - Glycoproteins/metabolism
MH  - Glycosylation
MH  - Membrane Glycoproteins/immunology/*metabolism
MH  - Molecular Sequence Data
MH  - Nuclear Envelope/*metabolism
MH  - Nuclear Pore Complex Proteins
MH  - Nuclear Proteins/immunology/*metabolism
MH  - Oocytes
MH  - Phosphates/*metabolism
MH  - Phosphorylation
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Isoforms/metabolism
MH  - Rats
MH  - Wheat Germ Agglutinins/metabolism
MH  - Xenopus laevis
EDAT- 1999/06/22 00:00
MHDA- 1999/06/22 00:01
CRDT- 1999/06/22 00:00
PHST- 1999/06/22 00:00 [pubmed]
PHST- 1999/06/22 00:01 [medline]
PHST- 1999/06/22 00:00 [entrez]
AID - 10.1006/abbi.1999.1237 [doi]
AID - S0003-9861(99)91237-7 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1999 Jul 1;367(1):51-60. doi: 10.1006/abbi.1999.1237.