Tonks, N. K., Neel, B. G.
(April 2001)
Combinatorial control of the specificity of protein tyrosine phosphatases.
Current Opinion in Cell Biology, 13 (2).
pp. 182-195.
ISSN 0955-0674
Abstract
Protein tyrosine phosphatases (PTPs), the enzymes that dephosphorylate tyrosyl phosphoproteins, were initially believed to be few in number and serve a 'housekeeping' role in signal transduction. Recent work indicates that this is totally incorrect. Instead, PTPs comprise a large superfamily whose members play critical roles in a wide variety of cellular processes. Moreover, PTPs exhibit exquisite substrate specificity in vivo. Recent evidence has led us to propose that members of the PTP family achieve selectivity through different combinations of specific targeting strategies and intrinsic catalytic domain specificity.
| Item Type: |
Paper
|
| Uncontrolled Keywords: |
GROWTH-FACTOR RECEPTOR
NUCLEOTIDE EXCHANGE FACTOR
CELL
SIGNAL-TRANSDUCTION
CRYSTAL-STRUCTURE
INSULIN-RECEPTOR
MAP-KINASE
MYOTUBULAR MYOPATHY
TUMOR-SUPPRESSOR
MICE LACKING
PTP-ALPHA |
| Subjects: |
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > Mitogen-activated protein kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase |
| CSHL Authors: |
|
| Communities: |
CSHL labs > Tonks lab |
| Depositing User: |
Matt Covey
|
| Date: |
April 2001 |
| Date Deposited: |
18 Dec 2013 19:31 |
| Last Modified: |
18 Dec 2013 19:31 |
| Related URLs: |
|
| URI: |
https://repository.cshl.edu/id/eprint/29014 |
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