Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein

Nick Carpino, Ryuji Kobayashi, Heesuk Zang, Yutaka Takahashi, Shiann Tarrng Jou, Jian Feng, Hideaki Nakajima, James N. Ihle

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

In a screen for proteins that interact with Jak2, we identified a previously uncharacterized 70-kDa protein and cloned the corresponding cDNA. The predicated sequence indicates that p70 contains an SH3 domain and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. p70 transcripts were found in all tissues examined. Similarly, when an antibody raised against a C-terminal peptide to analyze p70 protein expression was used, all murine tissues examined were found to express p70. To investigate the in vivo role of p70, we generated a p70-deficient mouse strain. Mice lacking p70 are viable, develop normally, and do not display any obvious abnormalities. No differences were detected in various hematological parameters, including bone marrow colony-forming ability, in response to cytokines that utilize Jak2. In addition, no impairment in B- and T-cell development and proliferative ability was detected.

Original languageEnglish
Pages (from-to)7491-7500
Number of pages10
JournalMolecular and Cellular Biology
Volume22
Issue number21
DOIs
Publication statusPublished - 2002 Nov
Externally publishedYes

Fingerprint

src Homology Domains
Organism Cloning
Complementary DNA
Phosphoglycerate Mutase
Proteins
Bone Marrow
Cytokines
T-Lymphocytes
Peptides
Antibodies

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein. / Carpino, Nick; Kobayashi, Ryuji; Zang, Heesuk; Takahashi, Yutaka; Jou, Shiann Tarrng; Feng, Jian; Nakajima, Hideaki; Ihle, James N.

In: Molecular and Cellular Biology, Vol. 22, No. 21, 11.2002, p. 7491-7500.

Research output: Contribution to journalArticle

Carpino, N, Kobayashi, R, Zang, H, Takahashi, Y, Jou, ST, Feng, J, Nakajima, H & Ihle, JN 2002, 'Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein', Molecular and Cellular Biology, vol. 22, no. 21, pp. 7491-7500. https://doi.org/10.1128/MCB.22.21.7491-7500.2002
Carpino, Nick ; Kobayashi, Ryuji ; Zang, Heesuk ; Takahashi, Yutaka ; Jou, Shiann Tarrng ; Feng, Jian ; Nakajima, Hideaki ; Ihle, James N. / Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein. In: Molecular and Cellular Biology. 2002 ; Vol. 22, No. 21. pp. 7491-7500.
@article{1acd1a76e90a43199323dae3748c42ae,
title = "Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein",
abstract = "In a screen for proteins that interact with Jak2, we identified a previously uncharacterized 70-kDa protein and cloned the corresponding cDNA. The predicated sequence indicates that p70 contains an SH3 domain and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. p70 transcripts were found in all tissues examined. Similarly, when an antibody raised against a C-terminal peptide to analyze p70 protein expression was used, all murine tissues examined were found to express p70. To investigate the in vivo role of p70, we generated a p70-deficient mouse strain. Mice lacking p70 are viable, develop normally, and do not display any obvious abnormalities. No differences were detected in various hematological parameters, including bone marrow colony-forming ability, in response to cytokines that utilize Jak2. In addition, no impairment in B- and T-cell development and proliferative ability was detected.",
author = "Nick Carpino and Ryuji Kobayashi and Heesuk Zang and Yutaka Takahashi and Jou, {Shiann Tarrng} and Jian Feng and Hideaki Nakajima and Ihle, {James N.}",
year = "2002",
month = "11",
doi = "10.1128/MCB.22.21.7491-7500.2002",
language = "English",
volume = "22",
pages = "7491--7500",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "21",

}

TY - JOUR

T1 - Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein

AU - Carpino, Nick

AU - Kobayashi, Ryuji

AU - Zang, Heesuk

AU - Takahashi, Yutaka

AU - Jou, Shiann Tarrng

AU - Feng, Jian

AU - Nakajima, Hideaki

AU - Ihle, James N.

PY - 2002/11

Y1 - 2002/11

N2 - In a screen for proteins that interact with Jak2, we identified a previously uncharacterized 70-kDa protein and cloned the corresponding cDNA. The predicated sequence indicates that p70 contains an SH3 domain and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. p70 transcripts were found in all tissues examined. Similarly, when an antibody raised against a C-terminal peptide to analyze p70 protein expression was used, all murine tissues examined were found to express p70. To investigate the in vivo role of p70, we generated a p70-deficient mouse strain. Mice lacking p70 are viable, develop normally, and do not display any obvious abnormalities. No differences were detected in various hematological parameters, including bone marrow colony-forming ability, in response to cytokines that utilize Jak2. In addition, no impairment in B- and T-cell development and proliferative ability was detected.

AB - In a screen for proteins that interact with Jak2, we identified a previously uncharacterized 70-kDa protein and cloned the corresponding cDNA. The predicated sequence indicates that p70 contains an SH3 domain and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. p70 transcripts were found in all tissues examined. Similarly, when an antibody raised against a C-terminal peptide to analyze p70 protein expression was used, all murine tissues examined were found to express p70. To investigate the in vivo role of p70, we generated a p70-deficient mouse strain. Mice lacking p70 are viable, develop normally, and do not display any obvious abnormalities. No differences were detected in various hematological parameters, including bone marrow colony-forming ability, in response to cytokines that utilize Jak2. In addition, no impairment in B- and T-cell development and proliferative ability was detected.

UR - http://www.scopus.com/inward/record.url?scp=0036837657&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036837657&partnerID=8YFLogxK

U2 - 10.1128/MCB.22.21.7491-7500.2002

DO - 10.1128/MCB.22.21.7491-7500.2002

M3 - Article

C2 - 12370296

AN - SCOPUS:0036837657

VL - 22

SP - 7491

EP - 7500

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 21

ER -