Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase.
We have molecularly cloned TPP36, a novel 36 kDa protein with 281 amino acids that was identified as a protein phosphorylated in B progenitor cells following stimulation with pervanadate/H(2)O(2). Analysis with anti-TPP36 antiserum revealed that TPP36 was expressed ubiquitously and had an isoform with 236 amino acids, designated TPP32. TPP36/32 were localized mainly in cytoplasm despite the presence of a typical nuclear localization signal sequence. These proteins were phosphorylated preferentially by Abl among a panel of tyrosine kinases examined. Phosphorylation of tyrosine 120 in TPP36/32 led to an apparent mobility shift in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting conformational change in the phosphorylated protein. Thus, TPP36/32 appear to be novel substrates of Abl tyrosine kinase.
Tsuchiya
Kiichiro
K
Department of Gastroenterology and Hepatology, Tokyo Medical and Dental University Graduate School, Japan.
Kawano
Youhei
Y
Kojima
Toshiyuki
T
Nagata
Kisaburo
K
Takao
Toshifumi
T
Okada
Masato
M
Shinohara
Hisaaki
H
Maki
Kazushige
K
Toyama-Sorimachi
Noriko
N
Miyasaka
Nobuyuki
N
Watanabe
Mamoru
M
Karasuyama
Hajime
H
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016374:Oncogene Proteins v-abl / Q000378:metabolism*; D009990:Oryzias; D010750:Phosphoproteins / Q000235:genetics* / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D016315:Proto-Oncogene Proteins c-abl; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014981:Xenopus
C473117:Cdv3 protein, mouse; D016374:Oncogene Proteins v-abl; D010750:Phosphoproteins; D020033:Protein Isoforms; D011505:Protein-Tyrosine Kinases; D016315:Proto-Oncogene Proteins c-abl