PMID- 10564280
OWN - NLM
STAT- MEDLINE
DCOM- 19991209
LR  - 20181113
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 11
DP  - 1999 Nov
TI  - The interaction and colocalization of Sam68 with the splicing-associated factor
      YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn).
PG  - 3909-26
AB  - Alternative pre-mRNA splicing patterns can change an extracellular stimulus, but 
      the signaling pathways leading to these changes are still poorly characterized.
      Here, we describe a tyrosine-phosphorylated nuclear protein, YT521-B, and show
      that it interacts with the nuclear transcriptosomal component scaffold attachment
      factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. Northern
      blot analysis demonstrated ubiquitous expression, but detailed RNA in situ
      analysis revealed cell type specificity in the brain. YT521-B protein is
      localized in the nucleoplasm and concentrated in 5-20 large nuclear dots.
      Deletion analysis demonstrated that the formation of these dots depends on the
      presence of the amino-terminal glutamic acid-rich domain and the
      carboxyl-terminal glutamic acid/arginine-rich region. We show that the latter
      comprises an important protein-protein interaction domain. The Src family kinase 
      p59(fyn)-mediated tyrosine phosphorylation of Sam68 negatively regulates its
      association with YT521-B, and overexpression of p59(fyn) dissolves nuclear dots
      containing YT521-B. In vivo splicing assays demonstrated that YT521-B modulates
      alternative splice site selection in a concentration-dependent manner. Together, 
      our data indicate that YT521-B and Sam68 may be part of a signal transduction
      pathway that influences splice site selection.
FAU - Hartmann, A M
AU  - Hartmann AM
AD  - Max-Planck-Institut of Neurobiology, Max-Planck-Institut of Biochemistry, D-82152
      Martinsried, Germany.
FAU - Nayler, O
AU  - Nayler O
FAU - Schwaiger, F W
AU  - Schwaiger FW
FAU - Obermeier, A
AU  - Obermeier A
FAU - Stamm, S
AU  - Stamm S
LA  - eng
SI  - GENBANK/AF144731
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (KHDRBS1 protein, human)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA Splicing Factors)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (YT521 protein, rat)
RN  - 0 (YTHDC1 protein, human)
RN  - 170974-22-8 (Serine-Arginine Splicing Factors)
RN  - EC 2.7.10.2 (FYN protein, human)
RN  - EC 2.7.10.2 (Fyn protein, rat)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn)
RN  - EC 2.7.10.2 (src-Family Kinases)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/metabolism
MH  - Cell Line
MH  - Cloning, Molecular
MH  - DNA-Binding Proteins
MH  - Fungal Proteins/metabolism
MH  - Humans
MH  - In Situ Hybridization
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*metabolism
MH  - Proto-Oncogene Proteins/*metabolism
MH  - Proto-Oncogene Proteins c-fyn
MH  - RNA Precursors/genetics
MH  - RNA Splicing/*genetics
MH  - RNA Splicing Factors
MH  - RNA-Binding Proteins/*metabolism
MH  - Rats
MH  - Sequence Deletion
MH  - Serine-Arginine Splicing Factors
MH  - Signal Transduction
MH  - Transfection
MH  - Yeasts
MH  - src-Family Kinases/metabolism
PMC - PMC25688
EDAT- 1999/11/17 00:00
MHDA- 1999/11/17 00:01
CRDT- 1999/11/17 00:00
PHST- 1999/11/17 00:00 [pubmed]
PHST- 1999/11/17 00:01 [medline]
PHST- 1999/11/17 00:00 [entrez]
AID - 10.1091/mbc.10.11.3909 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Nov;10(11):3909-26. doi: 10.1091/mbc.10.11.3909.