PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins
The PACSIN-related proteins are cytoplasmic adapter proteins with a common arrangement of domains and conserved regions. Here we report the cloning, sequencing, and expression of PACSIN 2, a novel member of the PACSIN protein family and accordingly rename the original PACSIN to PACSIN 1. The sequenc...
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| Veröffentlicht in: | FEBS letters 1999-07, Vol.454 (3), p.356-362 |
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| creator | Ritter, Brigitte Modregger, Jan Paulsson, Mats Plomann, Markus |
| description | The PACSIN-related proteins are cytoplasmic adapter proteins with a common arrangement of domains and conserved regions. Here we report the cloning, sequencing, and expression of PACSIN 2, a novel member of the PACSIN protein family and accordingly rename the original PACSIN to PACSIN 1. The sequences of the murine and human cDNAs reveal an open reading frame encoding a putative protein of 486 residues. Despite its high sequence similarity to PACSIN 1, PACSIN 2 is encoded by distinct transcripts in human and mouse, in particular displaying a ubiquitous expression pattern. Immunofluorescence microscopy of PACSIN 2-transfected NIH3T3 fibroblasts reveal a broad, vesicle-like cytoplasmic staining. In contrast to FAP52, another PACSIN-related protein derived from chicken brain, PACSIN 2 could not be detected at focal contacts. Taken together, these findings suggest that PACSIN 2 is a novel PACSIN isoform with similar domain and motif arrangement, but an unrestricted expression pattern, which may participate in the organization of the actin cytoskeleton and the regulation of vesicular traffic. |
| doi_str_mv | 10.1016/S0014-5793(99)00830-3 |
| format | Article |
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Here we report the cloning, sequencing, and expression of PACSIN 2, a novel member of the PACSIN protein family and accordingly rename the original PACSIN to PACSIN 1. The sequences of the murine and human cDNAs reveal an open reading frame encoding a putative protein of 486 residues. Despite its high sequence similarity to PACSIN 1, PACSIN 2 is encoded by distinct transcripts in human and mouse, in particular displaying a ubiquitous expression pattern. Immunofluorescence microscopy of PACSIN 2-transfected NIH3T3 fibroblasts reveal a broad, vesicle-like cytoplasmic staining. In contrast to FAP52, another PACSIN-related protein derived from chicken brain, PACSIN 2 could not be detected at focal contacts. 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Here we report the cloning, sequencing, and expression of PACSIN 2, a novel member of the PACSIN protein family and accordingly rename the original PACSIN to PACSIN 1. The sequences of the murine and human cDNAs reveal an open reading frame encoding a putative protein of 486 residues. Despite its high sequence similarity to PACSIN 1, PACSIN 2 is encoded by distinct transcripts in human and mouse, in particular displaying a ubiquitous expression pattern. Immunofluorescence microscopy of PACSIN 2-transfected NIH3T3 fibroblasts reveal a broad, vesicle-like cytoplasmic staining. In contrast to FAP52, another PACSIN-related protein derived from chicken brain, PACSIN 2 could not be detected at focal contacts. Taken together, these findings suggest that PACSIN 2 is a novel PACSIN isoform with similar domain and motif arrangement, but an unrestricted expression pattern, which may participate in the organization of the actin cytoskeleton and the regulation of vesicular traffic.</description><subject>Adapter protein</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>CDC15NT, CDC15 N-terminal</subject><subject>Cloning, Molecular</subject><subject>Cytoplasm - metabolism</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Complementary - isolation & purification</subject><subject>EH, eps15 homology</subject><subject>EST, expressed sequence tag</subject><subject>GAPDH, glyceraldehyde 3-phosphate dehydrogenase</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>NPF motif</subject><subject>PACSIN</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>PRD, proline-rich domain</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>SH3 domain</subject><subject>SH3, src homology 3</subject><subject>src Homology Domains</subject><subject>Syndapin</subject><subject>UTR, untranslated region</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kNtKAzEQQIMotlY_QdknUXA12dlkkycpxUuhXqD6HLLZWYzspW62hf696UUfhmFmDjPDIeSc0VtGmbibU8rSmGcKrpS6plQCjeGADJnMIIZUyEMy_EcG5MT7bxpqydQxGTCaApMgh-TlfTyZT1-j5CYyUdOusIpqrHPsoraM-i-M9vPS1K5ab5p23beLyvja2cgUZtEHdtG1PbrGn5Kj0lQez_Z5RD4fHz4mz_Hs7Wk6Gc9iC4z3MYLMeIIJtVnGshLAUizAKMHzFAXkPPyZGMlpzgujkhxSijwRFEMIHvgRudztDYd_luh7XTtvsapMg-3Sa6EUJELIAF7swWVeY6EXnatNt9Z_AgJwvwMwvLty2GlvHTYWC9eh7XXRugDrjXK9Va43PrVSeqtcA_wC8qJvDQ</recordid><startdate>19990709</startdate><enddate>19990709</enddate><creator>Ritter, Brigitte</creator><creator>Modregger, Jan</creator><creator>Paulsson, Mats</creator><creator>Plomann, Markus</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19990709</creationdate><title>PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins</title><author>Ritter, Brigitte ; Modregger, Jan ; Paulsson, Mats ; Plomann, Markus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-e38752e20c7717f33c0ed3a965b4e63b50182a850b5da92b340e5260e26065f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adapter protein</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>CDC15NT, CDC15 N-terminal</topic><topic>Cloning, Molecular</topic><topic>Cytoplasm - metabolism</topic><topic>DNA, Complementary - genetics</topic><topic>DNA, Complementary - isolation & purification</topic><topic>EH, eps15 homology</topic><topic>EST, expressed sequence tag</topic><topic>GAPDH, glyceraldehyde 3-phosphate dehydrogenase</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>NPF motif</topic><topic>PACSIN</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>PRD, proline-rich domain</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>SH3 domain</topic><topic>SH3, src homology 3</topic><topic>src Homology Domains</topic><topic>Syndapin</topic><topic>UTR, untranslated region</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ritter, Brigitte</creatorcontrib><creatorcontrib>Modregger, Jan</creatorcontrib><creatorcontrib>Paulsson, Mats</creatorcontrib><creatorcontrib>Plomann, Markus</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ritter, Brigitte</au><au>Modregger, Jan</au><au>Paulsson, Mats</au><au>Plomann, Markus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-07-09</date><risdate>1999</risdate><volume>454</volume><issue>3</issue><spage>356</spage><epage>362</epage><pages>356-362</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The PACSIN-related proteins are cytoplasmic adapter proteins with a common arrangement of domains and conserved regions. Here we report the cloning, sequencing, and expression of PACSIN 2, a novel member of the PACSIN protein family and accordingly rename the original PACSIN to PACSIN 1. The sequences of the murine and human cDNAs reveal an open reading frame encoding a putative protein of 486 residues. Despite its high sequence similarity to PACSIN 1, PACSIN 2 is encoded by distinct transcripts in human and mouse, in particular displaying a ubiquitous expression pattern. Immunofluorescence microscopy of PACSIN 2-transfected NIH3T3 fibroblasts reveal a broad, vesicle-like cytoplasmic staining. In contrast to FAP52, another PACSIN-related protein derived from chicken brain, PACSIN 2 could not be detected at focal contacts. 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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adapter protein Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Base Sequence CDC15NT, CDC15 N-terminal Cloning, Molecular Cytoplasm - metabolism DNA, Complementary - genetics DNA, Complementary - isolation & purification EH, eps15 homology EST, expressed sequence tag GAPDH, glyceraldehyde 3-phosphate dehydrogenase Humans Mice Molecular Sequence Data NPF motif PACSIN Phosphoproteins - genetics Phosphoproteins - metabolism PRD, proline-rich domain Proteins - genetics Proteins - metabolism Sequence Alignment SH3 domain SH3, src homology 3 src Homology Domains Syndapin UTR, untranslated region |
| title | PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins |
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