Literature DB >> 15464569

Receptor protein tyrosine phosphatases regulate neural development and axon guidance.

Sonya E Ensslen-Craig1, Susann M Brady-Kalnay.   

Abstract

The regulation of tyrosine phosphorylation is recognized as an important developmental mechanism. Both addition and removal of phosphate moieties on tyrosine residues are tightly regulated during development. Originally, most attention focused on the role of tyrosine kinases during development, but more recently, the developmental importance of tyrosine phosphatases has been gaining interest. Receptor protein tyrosine phosphatases (RPTPs) are of particular interest to developmental biologists because the extracellular domains of RPTPs are similar to those of cell adhesion molecules (CAMs). This suggests that RPTPs may have functions in development similar to CAMs. This review focuses on the role of RPTPs in development of the nervous system in processes such as axon guidance, synapse formation, and neural tissue morphogenesis.

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Year:  2004        PMID: 15464569     DOI: 10.1016/j.ydbio.2004.08.009

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  31 in total

Review 1.  Tumour suppressor function of protein tyrosine phosphatase receptor-T.

Authors:  Anthony Scott; Zhenghe Wang
Journal:  Biosci Rep       Date:  2011-10       Impact factor: 3.840

2.  Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons.

Authors:  Denice L Major; Susann M Brady-Kalnay
Journal:  Mol Cell Neurosci       Date:  2007-01-17       Impact factor: 4.314

3.  E-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent manner.

Authors:  Samantha A Oblander; Sonya E Ensslen-Craig; Frank M Longo; Susann M Brady-Kalnay
Journal:  Mol Cell Neurosci       Date:  2007-02-02       Impact factor: 4.314

4.  Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.

Authors:  Simon Lee; Clare Faux; Jennifer Nixon; Daniel Alete; John Chilton; Muhamed Hawadle; Andrew W Stoker
Journal:  Mol Cell Biol       Date:  2006-12-18       Impact factor: 4.272

5.  A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu.

Authors:  Susan M Burden-Gulley; Theresa J Gates; Adam M Burgoyne; Jennifer L Cutter; David T Lodowski; Shenandoah Robinson; Andrew E Sloan; Robert H Miller; James P Basilion; Susann M Brady-Kalnay
Journal:  Neoplasia       Date:  2010-04       Impact factor: 5.715

6.  N-cadherin is an in vivo substrate for protein tyrosine phosphatase sigma (PTPsigma) and participates in PTPsigma-mediated inhibition of axon growth.

Authors:  Roberta Siu; Chris Fladd; Daniela Rotin
Journal:  Mol Cell Biol       Date:  2006-10-23       Impact factor: 4.272

Review 7.  Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools.

Authors:  Sonya E L Craig; Susann M Brady-Kalnay
Journal:  Anticancer Agents Med Chem       Date:  2011-01       Impact factor: 2.505

8.  Tyrosine phosphatase PTPRD suppresses colon cancer cell migration in coordination with CD44.

Authors:  Kosuke Funato; Yusuke Yamazumi; Takeaki Oda; Tetsu Akiyama
Journal:  Exp Ther Med       Date:  2011-03-21       Impact factor: 2.447

9.  Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration.

Authors:  Adam M Burgoyne; Polly J Phillips-Mason; Susan M Burden-Gulley; Shenandoah Robinson; Andrew E Sloan; Robert H Miller; Susann M Brady-Kalnay
Journal:  Cancer Res       Date:  2009-08-18       Impact factor: 12.701

10.  Catalytic and substrate promiscuity: distinct multiple chemistries catalysed by the phosphatase domain of receptor protein tyrosine phosphatase.

Authors:  Bharath Srinivasan; Hanna Marks; Sreyoshi Mitra; David M Smalley; Jeffrey Skolnick
Journal:  Biochem J       Date:  2016-05-17       Impact factor: 3.857

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