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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification of myotubularin as the lipid phosphatase catalytic subunit
associated with the 3-phosphatase adapter protein, 3-PAP</title><author><name sortKey="Nandurkar, Harshal H" sort="Nandurkar, Harshal H" uniqKey="Nandurkar H" first="Harshal H." last="Nandurkar">Harshal H. Nandurkar</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation></author><author><name sortKey="Layton, Meredith" sort="Layton, Meredith" uniqKey="Layton M" first="Meredith" last="Layton">Meredith Layton</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Ludwig Institute of Medical Research, 3050 Parkville, Australia;</nlm:aff></affiliation></author><author><name sortKey="Laporte, Jocelyn" sort="Laporte, Jocelyn" uniqKey="Laporte J" first="Jocelyn" last="Laporte">Jocelyn Laporte</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Institute of Genetics and Molecular and Cellular Biology, 67404 Illkirch Cedex, France;</nlm:aff></affiliation></author><author><name sortKey="Selan, Carly" sort="Selan, Carly" uniqKey="Selan C" first="Carly" last="Selan">Carly Selan</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation></author><author><name sortKey="Corcoran, Lisa" sort="Corcoran, Lisa" uniqKey="Corcoran L" first="Lisa" last="Corcoran">Lisa Corcoran</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Biochemistry and Molecular Biology, Monash University, 3068 Clayton, Australia;</nlm:aff></affiliation></author><author><name sortKey="Caldwell, Kevin K" sort="Caldwell, Kevin K" uniqKey="Caldwell K" first="Kevin K." last="Caldwell">Kevin K. Caldwell</name><affiliation><nlm:aff wicri:cut="; and" id="N0x98a9910.0x9ba9050">Department of Neuroscience, University of New Mexico, Albuquerque, NM 87131</nlm:aff></affiliation></author><author><name sortKey="Mochizuki, Yasuhiro" sort="Mochizuki, Yasuhiro" uniqKey="Mochizuki Y" first="Yasuhiro" last="Mochizuki">Yasuhiro Mochizuki</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Haematology, Washington University Medical School, St. Louis, MO 63110</nlm:aff></affiliation></author><author><name sortKey="Majerus, Philip W" sort="Majerus, Philip W" uniqKey="Majerus P" first="Philip W." last="Majerus">Philip W. Majerus</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Haematology, Washington University Medical School, St. Louis, MO 63110</nlm:aff></affiliation></author><author><name sortKey="Mitchell, Christina A" sort="Mitchell, Christina A" uniqKey="Mitchell C" first="Christina A." last="Mitchell">Christina A. Mitchell</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Biochemistry and Molecular Biology, Monash University, 3068 Clayton, Australia;</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12847286</idno><idno type="pmc">166368</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC166368</idno><idno type="RBID">PMC:166368</idno><idno type="doi">10.1073/pnas.1033097100</idno><date when="2003">2003</date><idno type="wicri:Area/Pmc/Corpus">001070</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001070</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification of myotubularin as the lipid phosphatase catalytic subunit
associated with the 3-phosphatase adapter protein, 3-PAP</title><author><name sortKey="Nandurkar, Harshal H" sort="Nandurkar, Harshal H" uniqKey="Nandurkar H" first="Harshal H." last="Nandurkar">Harshal H. Nandurkar</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation></author><author><name sortKey="Layton, Meredith" sort="Layton, Meredith" uniqKey="Layton M" first="Meredith" last="Layton">Meredith Layton</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Ludwig Institute of Medical Research, 3050 Parkville, Australia;</nlm:aff></affiliation></author><author><name sortKey="Laporte, Jocelyn" sort="Laporte, Jocelyn" uniqKey="Laporte J" first="Jocelyn" last="Laporte">Jocelyn Laporte</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Institute of Genetics and Molecular and Cellular Biology, 67404 Illkirch Cedex, France;</nlm:aff></affiliation></author><author><name sortKey="Selan, Carly" sort="Selan, Carly" uniqKey="Selan C" first="Carly" last="Selan">Carly Selan</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation></author><author><name sortKey="Corcoran, Lisa" sort="Corcoran, Lisa" uniqKey="Corcoran L" first="Lisa" last="Corcoran">Lisa Corcoran</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">St. Vincent's Hospital, 3065 Melbourne, Australia;</nlm:aff></affiliation><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Biochemistry and Molecular Biology, Monash University, 3068 Clayton, Australia;</nlm:aff></affiliation></author><author><name sortKey="Caldwell, Kevin K" sort="Caldwell, Kevin K" uniqKey="Caldwell K" first="Kevin K." last="Caldwell">Kevin K. Caldwell</name><affiliation><nlm:aff wicri:cut="; and" id="N0x98a9910.0x9ba9050">Department of Neuroscience, University of New Mexico, Albuquerque, NM 87131</nlm:aff></affiliation></author><author><name sortKey="Mochizuki, Yasuhiro" sort="Mochizuki, Yasuhiro" uniqKey="Mochizuki Y" first="Yasuhiro" last="Mochizuki">Yasuhiro Mochizuki</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Haematology, Washington University Medical School, St. Louis, MO 63110</nlm:aff></affiliation></author><author><name sortKey="Majerus, Philip W" sort="Majerus, Philip W" uniqKey="Majerus P" first="Philip W." last="Majerus">Philip W. Majerus</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Haematology, Washington University Medical School, St. Louis, MO 63110</nlm:aff></affiliation></author><author><name sortKey="Mitchell, Christina A" sort="Mitchell, Christina A" uniqKey="Mitchell C" first="Christina A." last="Mitchell">Christina A. Mitchell</name><affiliation><nlm:aff id="N0x98a9910.0x9ba9050">Department of Biochemistry and Molecular Biology, Monash University, 3068 Clayton, Australia;</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Myotubularin is a dual-specific phosphatase that dephosphorylates
phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate.
Mutations in myotubularin result in the human disease X-linked myotubular
myopathy, characterized by persistence of muscle fibers that retain an
immature phenotype. We have previously reported the identification of the
3-phosphatase adapter protein (3-PAP), a catalytically inactive member of the
myotubularin gene family, which coprecipitates lipid phosphatidylinositol
3-phosphate-3-phosphatase activity from lysates of human platelets. We have
now identified myotubularin as the catalytically active 3-phosphatase subunit
interacting with 3-PAP. A 65-kDa polypeptide, coprecipitating with endogenous
3-PAP, was purified from SDS/PAGE, subjected to trypsin digestion, and
analyzed by collision-induced dissociation tandem MS. Three peptides derived
from human myotubularin were identified. Association between 3-PAP and
myotubularin was confirmed by reciprocal coimmunoprecipitation of both
endogenous and recombinant proteins expressed in K562 cells. Recombinant
myotubularin localized to the plasma membrane, causing extensive filopodia
formation. However, coexpression of 3-PAP with myotubularin led to attenuation
of the plasma membrane phenotype, associated with myotubularin relocalization
to the cytosol. Collectively these studies indicate 3-PAP functions as an
“adapter” for myotubularin, regulating myotubularin intracellular
location and thereby altering the phenotype resulting from myotubularin
overexpression.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="publisher-id">pnas</journal-id><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12847286</article-id><article-id pub-id-type="pmc">166368</article-id><article-id pub-id-type="publisher-id">1008660</article-id><article-id pub-id-type="doi">10.1073/pnas.1033097100</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Identification of myotubularin as the lipid phosphatase catalytic subunit
associated with the 3-phosphatase adapter protein, 3-PAP</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Nandurkar</surname><given-names>Harshal H.</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">*</xref><xref ref-type="corresp" rid="cor1">†</xref></contrib><contrib contrib-type="author"><name><surname>Layton</surname><given-names>Meredith</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">‡</xref></contrib><contrib contrib-type="author"><name><surname>Laporte</surname><given-names>Jocelyn</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">§</xref></contrib><contrib contrib-type="author"><name><surname>Selan</surname><given-names>Carly</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">*</xref></contrib><contrib contrib-type="author"><name><surname>Corcoran</surname><given-names>Lisa</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">*</xref><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">¶</xref></contrib><contrib contrib-type="author"><name><surname>Caldwell</surname><given-names>Kevin K.</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">∥</xref></contrib><contrib contrib-type="author"><name><surname>Mochizuki</surname><given-names>Yasuhiro</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">**</xref></contrib><contrib contrib-type="author"><name><surname>Majerus</surname><given-names>Philip W.</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">**</xref></contrib><contrib contrib-type="author"><name><surname>Mitchell</surname><given-names>Christina A.</given-names></name><xref ref-type="aff" rid="N0x98a9910.0x9ba9050">¶</xref></contrib></contrib-group><aff id="N0x98a9910.0x9ba9050"><label>*</label>St. Vincent's Hospital, 3065 Melbourne, Australia;<label>‡</label>Ludwig Institute of Medical Research, 3050 Parkville, Australia;<label>§</label>Institute of Genetics and Molecular and Cellular Biology, 67404 Illkirch Cedex, France;<label>¶</label>Department of Biochemistry and Molecular Biology, Monash University, 3068 Clayton, Australia;<label>∥</label>Department of Neuroscience, University of New Mexico, Albuquerque, NM 87131; and<label>**</label>Department of Haematology, Washington University Medical School, St. Louis, MO 63110</aff><author-notes><fn id="cor1"><label>†</label><p>To whom correspondence should be addressed. E-mail:
<email>Harshal.Nandurkar@svhm.org.au</email>.
</p></fn><fn><p>Contributed by Philip W. Majerus, May 21, 2003</p></fn></author-notes><pub-date pub-type="ppub"><day>22</day><month>7</month><year>2003</year></pub-date><pub-date pub-type="epub"><day>7</day><month>7</month><year>2003</year></pub-date><volume>100</volume><issue>15</issue><fpage>8660</fpage><lpage>8665</lpage><copyright-statement>Copyright © 2003, The National Academy of
Sciences</copyright-statement><copyright-year>2003</copyright-year><abstract><p>Myotubularin is a dual-specific phosphatase that dephosphorylates
phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate.
Mutations in myotubularin result in the human disease X-linked myotubular
myopathy, characterized by persistence of muscle fibers that retain an
immature phenotype. We have previously reported the identification of the
3-phosphatase adapter protein (3-PAP), a catalytically inactive member of the
myotubularin gene family, which coprecipitates lipid phosphatidylinositol
3-phosphate-3-phosphatase activity from lysates of human platelets. We have
now identified myotubularin as the catalytically active 3-phosphatase subunit
interacting with 3-PAP. A 65-kDa polypeptide, coprecipitating with endogenous
3-PAP, was purified from SDS/PAGE, subjected to trypsin digestion, and
analyzed by collision-induced dissociation tandem MS. Three peptides derived
from human myotubularin were identified. Association between 3-PAP and
myotubularin was confirmed by reciprocal coimmunoprecipitation of both
endogenous and recombinant proteins expressed in K562 cells. Recombinant
myotubularin localized to the plasma membrane, causing extensive filopodia
formation. However, coexpression of 3-PAP with myotubularin led to attenuation
of the plasma membrane phenotype, associated with myotubularin relocalization
to the cytosol. Collectively these studies indicate 3-PAP functions as an
“adapter” for myotubularin, regulating myotubularin intracellular
location and thereby altering the phenotype resulting from myotubularin
overexpression.</p></abstract></article-meta><notes><fn-group><fn><p>Abbreviations: PtdIns(3)P, phosphatidylinositol 3-phosphate;
PtdIns(3,5)P<sub>2</sub>, phosphatidylinositol 3,5-bisphosphate; 3-PAP,
3-phosphatase adapter protein; HA, hemagglutinin; SID, SET-interacting
domain.</p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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