<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2022000100314</article-id>
<article-id pub-id-type="doi">10.22201/fesz.23958723e.2022.503</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[PTP-PEST: Vías de señalización y su importancia como blanco terapéutico en cáncer]]></article-title>
<article-title xml:lang="en"><![CDATA[PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Manzanita-Quintero]]></surname>
<given-names><![CDATA[Katya]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Lee-Rivera]]></surname>
<given-names><![CDATA[Irene]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[López]]></surname>
<given-names><![CDATA[Edith]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[López-Colomé]]></surname>
<given-names><![CDATA[Ana María]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Instituto de Fisiología Celular Departamento de Neuropatología Molecular]]></institution>
<addr-line><![CDATA[Ciudad de México ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2022</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2022</year>
</pub-date>
<volume>25</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2022000100314&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2022000100314&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2022000100314&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen La fosfatasa de tirosina PTP-PEST, también llamada PTPN12, es una proteína que se expresa de forma ubicua, y se regula por fosforilación en los residuos de serina y treonina. El gen PTPN12, en humanos, se localiza en el cromosoma 7q11.23. La proteína codificada está formada por una región N-terminal, seguida de un dominio catalítico de fosfatasa de tirosina (PTP, por sus siglas en inglés) y una cola C-terminal que contiene secuencias ricas en prolina, ácido glutámico, serina y treonina (PEST), así como, una secuencia NPLH (asparagina, prolina, leucina, histidina) que es un sitio de anclaje para las proteínas involucradas en la transducción de señales. La PTP-PEST regula procesos fisiológicos como la migración celular, la respuesta inmune, y la actividad neuronal, a través de la desfosforilación de múltiples sustratos entre los que se cuentan proteínas adaptadoras del citoesqueleto como la paxilina, y otras involucradas en diferentes vías de señalización, algunas de las cuales aún no han sido completamente elucidadas. Se ha demostrado la alteración de la PTP-PEST en diferentes enfermedades como el cáncer, por lo que se ha estudiado como un posible blanco terapéutico. Esta revisión se enfoca en la clasificación, estructura y el papel tanto fisiológico como patológico de la PTP-PEST.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Protein tyrosine phosphatase PTP-PEST, also known as PTPN12, is ubiquitously expressed and it is regulated by the phosphorylation of serine and threonine residues. PTPN12 gene is located, in humans, in chromosome 7q11.23. The coded protein comprises an N-terminal region, followed by a tyrosine phosphatase catalytic domain, and a C-terminal tail containing sequences rich in proline, glutamic acid, serine and threonine (PEST), as well as an NPLH (asparagine, proline, leucine, histidine) sequence that functions as a docking site for proteins involved in signal transduction. PTP-PEST regulates various physiological processes such as cell migration, immune response and neuronal activity by phosphorylating multiple substrates; among them several cytoskeleton adaptor proteins such as paxillin, and others involved in signal transduction pathways, some of which have not been completely elucidated. PTP-PEST is altered in several diseases such as cancer, and has been studied as a therapeutic target. This review focuses on its classification, structure and both its physiological and pathological roles.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[cinasas]]></kwd>
<kwd lng="es"><![CDATA[fosfatasas de tirosina]]></kwd>
<kwd lng="es"><![CDATA[transducción de señales]]></kwd>
<kwd lng="es"><![CDATA[adhesión focal]]></kwd>
<kwd lng="es"><![CDATA[migración celular]]></kwd>
<kwd lng="en"><![CDATA[kinases]]></kwd>
<kwd lng="en"><![CDATA[tyrosine phosphatases]]></kwd>
<kwd lng="en"><![CDATA[signal transduction]]></kwd>
<kwd lng="en"><![CDATA[focal adhesion]]></kwd>
<kwd lng="en"><![CDATA[cell migration]]></kwd>
</kwd-group>
</article-meta>
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