PMID- 10600535
OWN - NLM
STAT- MEDLINE
DCOM- 20000118
LR  - 20071115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 266
IP  - 2
DP  - 1999 Dec 20
TI  - Characterization of newly identified four isoforms for a putative cytosolic
      protein tyrosine phosphatase PTP36.
PG  - 523-31
AB  - In the course of determining the expression profiles of protein tyrosine
      phosphatases in lactating mammary gland, we found the expression of an isoform
      for a putative cytosolic and cytoskeleton-associated protein tyrosine phosphatase
      PTP36. Further detailed RT-PCR and Northern blot analyses revealed the expression
      of several isoforms for PTP36 in a tissue-dependent manner. We have cloned the
      cDNAs encoding four truncated isoforms for PTP36 and designated PTP36-A, -B, -C, 
      and -D, respectively. PTP36-A and -C had new sequences generated due to
      frameshift, whereas PTP36-B and -D were in-frame variants. Gly- and Glu-rich
      domains and a putative PTP domain were missing from PTP36-A, but the band 4.1
      domain remained. PTP36-B retained the band 4.1 and PTP domains but lacked Pro-,
      Gly- and Glu-rich domains. Most domain structures were lacking in PTP36-C and -D.
      Interestingly, PTP36-C contained an incomplete band 4.1 domain, but the newly
      created sequence exhibited high homology to human nebulette, which was also
      suggested to associate with cytoskeletons. When transiently expressed in COS7 and
      HEK293 cells, not only the wild type but also all the isoforms were recovered in 
      Triton X-100-insoluble cytoskeleton-associated fractions and this distribution
      was not affected by mechanical cell detachment and treatment with a kinase
      inhibitor staurosporine. Such cellular distribution of PTP36 was also observed in
      stable COS7 clones. Further studies using deletion mutants suggested that the
      first 30 amino acids as well as the band 4.1 domain of PTP36 were involved in
      association with Triton X-100 insoluble cytoskeletons. Tissue-dependent
      expression and deletion in domain structures might reflect the biological
      significance of the isoforms for PTP36 in certain physiological conditions.
CI  - Copyright 1999 Academic Press.
FAU - Aoyama, K
AU  - Aoyama K
AD  - Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho,
      Chikusa-ku, Nagoya, 464-8601, Japan.
FAU - Matsuda, T
AU  - Matsuda T
FAU - Aoki, N
AU  - Aoki N
LA  - eng
SI  - GENBANK/AF170902
SI  - GENBANK/AF170903
SI  - GENBANK/AF170904
SI  - GENBANK/AF170905
PT  - Journal Article
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Isoenzymes)
RN  - 0 (RNA, Messenger)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Cytoskeletal Proteins/chemistry/genetics
MH  - Humans
MH  - Isoenzymes/chemistry/genetics
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Tyrosine Phosphatases/chemistry/*genetics
MH  - RNA, Messenger/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Transfection
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1006/bbrc.1999.1845 [doi]
AID - S0006-291X(99)91845-4 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Dec 20;266(2):523-31. doi:
      10.1006/bbrc.1999.1845.