Abstract:
:Dual-specificity phosphatases (DSPs), which dephosphorylate proteins at Ser/Thr as well as Tyr residues, are thought to be involved in critical signaling events such as control of MAP kinases (MAPKs). We have isolated the cDNA for a novel DSP and termed it low molecular mass DSP-4 (LDP-4). LDP-4 is composed of 211 amino acids with a predicted molecular mass of 23.9-kDa. Northern blot analysis using various mouse tissues showed that the LDP-4 transcript was expressed exclusively in brain. In situ hybridization showed that brain expression of LDP-4 was ubiquitous except for the hippocampus. When expressed in COS-7 cells, FLAG-tagged LDP-4 protein was present within the nucleus and Golgi apparatus. LDP-4 expression did not reduce phosphorylation levels of MAPKs, but rather evoked activation of JNK and p38.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Takagaki K,Shima H,Tanuma N,Nomura M,Satoh T,Watanabe M,Kikuchi Kdoi
10.1007/s11010-006-9313-5subject
Has Abstractpub_date
2007-02-01 00:00:00pages
177-84issue
1-2eissn
0300-8177issn
1573-4919journal_volume
296pub_type
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