PMID- 17050672
OWN - NLM
STAT- MEDLINE
DCOM- 20070212
LR  - 20190816
IS  - 1541-7786 (Print)
IS  - 1541-7786 (Linking)
VI  - 4
IP  - 10
DP  - 2006 Oct
TI  - Phosphorylation of the menin tumor suppressor protein on serine 543 and serine 
      583.
PG  - 793-801
AB  - Multiple endocrine neoplasia type 1 (MEN-1) is a heritable syndrome typified by 
      tumors in multiple endocrine organs, including the pituitary, parathyroids, and 
      pancreatic islets. MEN-1 is attributable to mutations in the MEN1 
      tumor-suppressor gene that encodes the menin protein. Recent studies have 
      implicated menin in transcriptional regulation and in covalent histone 
      modification; however, little is known about modifications of the menin protein. 
      Here, we report that menin is subject to phosphorylation on serine residues, 
      including Ser543 and Ser583. Phosphorylation-defective mutants of either or both 
      of these residues retain the associated histone methyltransferase activity of 
      menin, as well as binding to the trithorax complex members Ash2L, Rbbp5, and MLL2 
      and to RNA polymerase II. Chromatin immunoprecipitation experiments reveal that 
      binding of menin to the Hoxc8 locus is not affected by phosphorylation on Ser543 
      or Ser583.
FAU - MacConaill, Laura E
AU  - MacConaill LE
AD  - Department of Medical Oncology, Dana-Farber Cancer Institute, 44 Binney St., 
      Boston, MA 02115, USA.
FAU - Hughes, Christina M
AU  - Hughes CM
FAU - Rozenblatt-Rosen, Orit
AU  - Rozenblatt-Rosen O
FAU - Nannepaga, Suraj
AU  - Nannepaga S
FAU - Meyerson, Matthew
AU  - Meyerson M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cancer Res
JT  - Molecular cancer research : MCR
JID - 101150042
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Homeodomain Proteins)
RN  - 0 (KMT2D protein, human)
RN  - 0 (MEN1 protein, human)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 452VLY9402 (Serine)
RN  - EC 2.1.1.- (Histone Methyltransferases)
RN  - EC 2.1.1.- (Protein Methyltransferases)
RN  - EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
SB  - IM
MH  - Cell Differentiation
MH  - Cells, Cultured
MH  - Chromatin Immunoprecipitation
MH  - DNA Damage
MH  - DNA-Binding Proteins/*metabolism
MH  - HL-60 Cells
MH  - Histone Methyltransferases
MH  - Histone-Lysine N-Methyltransferase/*metabolism
MH  - Homeodomain Proteins/metabolism
MH  - Humans
MH  - Neoplasm Proteins/*metabolism
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein Isoforms
MH  - Protein Methyltransferases
MH  - Proto-Oncogene Proteins/*metabolism
MH  - *Serine
MH  - Transfection
MH  - Tumor Suppressor Proteins/*metabolism
EDAT- 2006/10/20 09:00
MHDA- 2007/02/13 09:00
CRDT- 2006/10/20 09:00
PHST- 2006/10/20 09:00 [pubmed]
PHST- 2007/02/13 09:00 [medline]
PHST- 2006/10/20 09:00 [entrez]
AID - 4/10/793 [pii]
AID - 10.1158/1541-7786.MCR-06-0123 [doi]
PST - ppublish
SO  - Mol Cancer Res. 2006 Oct;4(10):793-801. doi: 10.1158/1541-7786.MCR-06-0123.