PMID- 10413518
OWN - NLM
STAT- MEDLINE
DCOM- 19990915
LR  - 20091119
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 38
IP  - 29
DP  - 1999 Jul 20
TI  - Identification of phosphorylation sites in native lamina-associated polypeptide 2
      beta.
PG  - 9426-34
AB  - Lamina-associated polypeptide 2 beta (LAP 2 beta), an integral protein of the
      inner nuclear membrane, appears to be involved in the spatial organization of the
      interface between nucleoplasma, lamina, and nuclear envelope. Its ability to
      interact with other proteins and the structural integrity of the nuclear envelope
      is probably regulated by phosphorylation. Here, we report nonmitotic LAP 2 beta
      phosphorylation sites that are phosphorylated in the native protein when purified
      from nuclear envelopes of mouse neuroblastoma Neuro2a cells. Five phosphorylation
      sites were detected by nano-electrospray mass spectrometric analysis of tryptic
      LAP 2 beta peptides using parent ion scans specific for phosphopeptides. By mass 
      spectrometric sequencing of these peptides, we identified as phosphorylated
      residues Thr 74, Thr 159, Ser 176, and Ser 179. Two of the phosphorylation sites,
      Thr 74 (within a region known to bind chromatin) and Thr 159, are part of
      consensus sequences of proline-directed kinases. Ser 179 is part of a consensus
      site for protein kinase C which is able to highly phosphorylate LAP 2 beta in
      vitro. Three phosphorylation sites, Thr 159, Ser 176, and Ser 179, are located
      within a stretch of 20 amino acids, thereby forming a highly phosphorylated
      protein domain which may integrate signaling by multiple protein kinases.
      Additionally, we identified for the first time at the protein level the LAP 2
      splice variant LAP 2 epsilon in nuclear envelopes.
FAU - Dreger, M
AU  - Dreger M
AD  - AG Neurochemie, Institut fur Biochemie, Freie Universitat Berlin, Germany.
FAU - Otto, H
AU  - Otto H
FAU - Neubauer, G
AU  - Neubauer G
FAU - Mann, M
AU  - Mann M
FAU - Hucho, F
AU  - Hucho F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphopeptides)
RN  - 0 (lamina-associated polypeptide 2)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *DNA-Binding Proteins
MH  - Membrane Proteins/isolation & purification/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neoplasm Proteins/isolation & purification/metabolism
MH  - Neuroblastoma
MH  - Nuclear Envelope/enzymology/metabolism
MH  - Nuclear Proteins/isolation & purification/*metabolism
MH  - Phosphopeptides/isolation & purification/metabolism
MH  - Phosphorylation
MH  - Protein Kinase C/metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Protein-Tyrosine Kinases/metabolism
MH  - Substrate Specificity
MH  - Tumor Cells, Cultured
EDAT- 1999/07/22 00:00
MHDA- 1999/07/22 00:01
CRDT- 1999/07/22 00:00
PHST- 1999/07/22 00:00 [pubmed]
PHST- 1999/07/22 00:01 [medline]
PHST- 1999/07/22 00:00 [entrez]
AID - 10.1021/bi990645f [doi]
AID - bi990645f [pii]
PST - ppublish
SO  - Biochemistry. 1999 Jul 20;38(29):9426-34. doi: 10.1021/bi990645f.