Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Hendriks, Wiljan; Schepens, Jan; Bächner, Dietmar; Rijss, J.P.L.; Zeeuwen, Patrick L.J.M.; Zechner, Ulrich; Hameister, Horst; Wieringa, Bé

doi:10.1002/jcb.240590403

Cited by 51 publications

(56 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, this protein tyrosine phosphatase is expressed within epithelial cells and thus shows an overlapping expression pattern with the APC protein (Hendriks et al, 1995;Midgley et al, 1997). Using the two-hybrid system we checked all ®ve PDZ domains of PTP-BL for interaction with the last 73 amino acids of the APC protein.…”

Section: Resultsmentioning

confidence: 99%

“…We expressed the protein tyrosine phosphatase domain and the catalytically inactive version (corresponding to amino acids: 2108 ± 2460, (Hendriks et al, 1995)) in fusion with glutathione-S-transferase. Catalytically inactive phosphatase domain was generated using PCR-based site directed mutagenesis by replacing cysteine 2374 by serine using primers: CS up: GCTGGAGTGTGTGATGACTGGGCC-CG, CS down: CCCAGTCATCACACACTCCAGCGCTG-GCATTGGACGCTC.…”

Section: In Vitro Dephosphorylation Assay Of B-cateninmentioning

confidence: 99%

“…Here we describe an interaction of the APC protein with a protein tyrosine phosphatase, PTP-BL (Banville et al, 1994;Maekawa et al, 1994;Saras et al, 1994;Hendriks et al, 1995). PTP-BL is a nontransmembrane protein tyrosine phosphatase implicated in the modulation of the cytoskeleton.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Erdmann

Kuhlmann²,

Leßmann

et al. 2000

Oncogene

View full text Add to dashboard Cite

Mutations of the tumor suppressor protein APC (Adenomatous Polyposis Coli) are linked to familiar and sporadic human colon cancer. Here we describe a novel interaction between the APC protein and the protein tyrosine phosphatase PTP-BL carrying ®ve PDZ protein ± protein interaction domains. Exclusively, the second PDZ domain (PDZ2) of PTP-BL is binding to the extreme C-terminus of the APC protein, as determined by yeast two-hybrid studies. Using surface plasmon resonance analysis we established a dissociation constant (K D ) of 8.1610 79 M. We ®nd that a naturally occurring splice insertion of ®ve amino acids (PDZ2b) abolishes its binding a nity to the APC protein. The in vivo interaction between PTP-BL and the APC protein was shown by coprecipitation experiments in transfected COS cells. Furthermore, in cultured epithelial Madine Carnine Kidney cells the subcellular colocalization was demonstrated for the nucleus and also for the tips of cellular extensions. The interaction of the APC protein with a protein tyrosine phosphatase may indirectly modulate the steady state levels of tyrosine phosphorylations of associated proteins, such as b-catenin playing a major role in the regulation of cell division, migration and cell adhesion. Oncogene (2000) 19, 3894 ± 3901.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: In Vitro Dephosphorylation Assay Of B-cateninmentioning

confidence: 99%

See 1 more Smart Citation

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Erdmann

Kuhlmann²,

Leßmann

et al. 2000

Oncogene

View full text Add to dashboard Cite

show abstract

“…Protein tyrosine phosphatase nonreceptor type 13 (PTPN13; also known as FAP1, PTPL1, PTP1E, PTP-BL or PTP-BAS) is a 250 kDa protein tyrosine phosphatase expressed in most cells (Hendriks et al, 1995). The protein is composed of a Cterminal catalytic domain and a large N terminus.…”

Section: Discussionmentioning

confidence: 99%

Potential role of protein tyrosine phosphatase nonreceptor type 13 in the control of oocyte meiotic maturation

Nedachi

Conti

2004

Development

View full text Add to dashboard Cite

Protein tyrosine phosphatase nonreceptor type 13 (PTPN13) is a tyrosine phosphatase with multiple interacting domains that has been implicated previously in the regulation of apoptosis. We provide evidence that PTPN13 plays an important role in the control of the meiotic cell cycle. A cDNA coding for PTPN13 was isolated during the screening for the substrate of protein kinase A expressed in mammalian oocytes. PTPN13 is expressed in both mouse and Xenopus oocytes and is a substrate for protein kinase A in vitro and in vivo. Expression of a truncated constitutively-active PTPN13 in Xenopus oocytes synergizes with progesterone in the induction of germinal vesicle breakdown, the translation of Mos, the phosphorylation of Erk and the dephosphorylation of Cdc2. The phosphatase activity of PTPN13 is required for this synergism. Oocyte injection with specific small interference RNA downregulates the expression of mRNA for PTPN13 and blocks oocyte maturation induced by progesterone, a blockade that can be overcome by Cdc25 overexpression. These findings indicate that PTPN13 is involved in the regulation of the meiotic cell cycle.

show abstract

“…18,39 -42 Its function remains unclear, but it has been shown to be constitutively expressed by polarized epithelial cells in a variety of tissues, including lung, epidermis, and gut. 40 PTPL1 has multiple protein-protein interaction domains in addition to its single PTPase domain. At the amino terminus is a band 4.1-like domain, suggesting cytoskeletal localization.…”

Section: Discussionmentioning

confidence: 99%

Protein-Tyrosine Phosphatases in the Vessel Wall

Wright

Seifert

Bowen‐Pope

2000

ATVB

View full text Add to dashboard Cite

Abstract-Many protein-tyrosine phosphatases (PTPases) have now been identified, but little is known about PTPase expression and regulation in vascular tissue and in vascular disease. Polymerase chain reaction (PCR) amplification and cDNA fingerprinting of PTPase catalytic domains, combined with random sequencing of PCR product libraries, identified 18 (8 receptor-like and 10 cytosolic) PTPases in the rat carotid artery and revealed differential expression of 5 of these PTPases during neointima formation after balloon catheter injury. In situ hybridization was used to localize mRNA expression in vessel cross sections for the 5 differentially expressed PTPases. This revealed that for 3 PTPases (SHP1, CD45, and PTP␤), differential transcript abundance was due to appearance/loss of the cell types by which they were expressed (leukocytes for SHP1 and CD45, endothelial cells for PTP␤). However, mRNA expression of 2 PTPases (PTPL1 and PTP1B) was specifically upregulated by proliferating and migrating smooth muscle cells (SMCs) in characteristic temporal and regional patterns in response to vessel damage. Quantitative PCR analysis showed that PTP1B and PTPL1 were induced Ϸ30-fold and Ϸ60-fold, respectively, by 2 weeks after injury in the damaged vessels compared with the uninjured vessels. PTP1B was rapidly upregulated in the media after vessel injury and remained highly expressed in the developing neointima. By contrast, PTPL1 expression did not increase dramatically until the SMCs had migrated into the intima. The differential expression of PTP1B and PTPL1 by SMCs after injury suggests roles for these PTPases in the regulation of vessel wall remodeling. Key Words: protein-tyrosine phosphatase Ⅲ smooth muscle cells Ⅲ injury Ⅲ neointima Ⅲ carotid arteries A cute arterial injury stimulates smooth muscle cell (SMC) proliferation in the media, followed by the migration of SMCs into the intima. These events result in vessel wall remodeling and the formation of a neointima. Multiple secreted growth factors mediate the SMC proliferation and migration that occurs after balloon catheter injury of the normal rat carotid artery. Basic fibroblast growth factor appears to be the major mitogen driving early medial SMC proliferation, whereas platelet-derived growth factor has a lesser effect on SMC replication but plays a major role in promoting the migration of SMCs into the intima. [1][2][3] Protein-tyrosine phosphatases (PTPases) reverse the activity of growth factor receptor tyrosine kinases and likely play important roles in the vessel wall; however, little is known of the identity of PTPases expressed by vascular tissue, and less is known about the potential roles of specific PTPases in active remodeling. Approximately 70 to 80 PTPases have been cloned and described. 4 The family is broadly divided between receptor-like and cytosolic enzymes and is further divided by the similarities of accessory and regulatory motifs. 5 The receptor PTPases generally contain an extracellular region with adhesion-like motifs, a single membranes...

show abstract

Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Cited by 51 publications

References 48 publications

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Potential role of protein tyrosine phosphatase nonreceptor type 13 in the control of oocyte meiotic maturation

Protein-Tyrosine Phosphatases in the Vessel Wall

Contact Info

Product

Resources

About