The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)

Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two pu...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1995-12, Vol.270 (52), p.30853-30856
Main Authors: Fiore, Francesca, Zambrano, Nicola, Minopoli, Giuseppina, Donini, Virgilio, Duilio, Angela, Russo, Tommaso
Format: Article
Language:English
Subjects:
Alzheimer Disease - metabolism
Amino Acid Sequence
Amyloid beta-Protein Precursor - metabolism
Animals
DNA, Complementary
Humans
Mice
Molecular Sequence Data
Nerve Tissue Proteins - metabolism
Nuclear Proteins - metabolism
PC12 Cells
Phosphotyrosine - metabolism
Protein Binding
Rats
Sequence Homology, Amino Acid
src Homology Domains
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3
cites cdi_FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3
container_end_page 30856
container_issue 52
container_start_page 30853
container_title The Journal of biological chemistry
container_volume 270
creator Fiore, Francesca
Zambrano, Nicola
Minopoli, Giuseppina
Donini, Virgilio
Duilio, Angela
Russo, Tommaso
description Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two putative PID/PTB domains of Fe65 were used to construct glutathione S-transferase-Fe65 fusion proteins. Co-precipitation experiments demonstrated that the Fe65 PID/PTB domains interacted with several proteins of apparent molecular mass 135, 115, 105, and 51 kDa. The region of Fe65 containing the PID/PTB domains was used as a bait to screen a human brain cDNA library in yeast by the two-hybrid system. Three different cDNA clones were isolated, two of which contain overlapping segments of the cDNA encoding the COOH terminus of the Alzheimer's β-amyloid-precursor protein (APP), that represents the short intracellular domain of this membrane protein. The third clone contains a cDNA fragment coding for the COOH terminus of the human counterpart of a mouse β-amyloid-like precursor protein. The alignment of the three APP encoding cDNA fragments found in the screening suggests that the region of APP involved in the binding is centered on the NPTY sequence, which is analogous to that present in the intracellular domains of the growth factor receptors interacting with the PID/PTB domain of Shc.
doi_str_mv 10.1074/jbc.270.52.30853
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77785146</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925817353309</els_id><sourcerecordid>17024127</sourcerecordid><originalsourceid>FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3</originalsourceid><addsrcrecordid>eNqFUctu1DAUtRBVGQp7NkheIKCLTG3HjjPshkIfUiUqKBI7y3GuJ66SeLCTVsMX8Af8EF_Cl9TzUIUqIbyx7PO4R_cg9IKSKSWSH11XZsokmQo2zUkp8kdoQkmZZ7mg3x6jCSGMZjMmyifoaYzXJB0-o_toP1FlnssJ-n3VAP4MC-f7iL3FQ3qeQCHwZfADuB6f-c63fuHHiAe_gS8bH5eNH1bBR9cDPu8HCNoMyeLoIfbe9bXrF_iD73QySwO-NGbzu7FK0qSEth1bHf4irbF5-6MB10F4E_G8W7Xe1SkUmDFEH-7jvf3z89fhM7RndRvh-e4-QF9PPl4dn2UXn07Pj-cXmeFcDllecVMUlrOi4paVAqyZ6ZoT0IW2vBRGMCullmCosBZACAulKHlVWWm0NfkBer31XQb_fYQ4qM7FdXzdQ1qQklKWgvLiv0QqCeOUyUQkW6JJC4sBrFoG1-mwUpSodcMqNaxSw0owtWk4SV7uvMeqg_pesKs04a-2eOMWza0LoCrnTQPdQ5t3Wxqkhd04CCoaB72BOknMoGrv_p3hDvjmxpk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17024127</pqid></control><display><type>article</type><title>The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)</title><source>BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS</source><creator>Fiore, Francesca ; Zambrano, Nicola ; Minopoli, Giuseppina ; Donini, Virgilio ; Duilio, Angela ; Russo, Tommaso</creator><creatorcontrib>Fiore, Francesca ; Zambrano, Nicola ; Minopoli, Giuseppina ; Donini, Virgilio ; Duilio, Angela ; Russo, Tommaso</creatorcontrib><description>Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two putative PID/PTB domains of Fe65 were used to construct glutathione S-transferase-Fe65 fusion proteins. Co-precipitation experiments demonstrated that the Fe65 PID/PTB domains interacted with several proteins of apparent molecular mass 135, 115, 105, and 51 kDa. The region of Fe65 containing the PID/PTB domains was used as a bait to screen a human brain cDNA library in yeast by the two-hybrid system. Three different cDNA clones were isolated, two of which contain overlapping segments of the cDNA encoding the COOH terminus of the Alzheimer's β-amyloid-precursor protein (APP), that represents the short intracellular domain of this membrane protein. The third clone contains a cDNA fragment coding for the COOH terminus of the human counterpart of a mouse β-amyloid-like precursor protein. The alignment of the three APP encoding cDNA fragments found in the screening suggests that the region of APP involved in the binding is centered on the NPTY sequence, which is analogous to that present in the intracellular domains of the growth factor receptors interacting with the PID/PTB domain of Shc.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.52.30853</identifier><identifier>PMID: 8537337</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alzheimer Disease - metabolism ; Amino Acid Sequence ; Amyloid beta-Protein Precursor - metabolism ; Animals ; DNA, Complementary ; Humans ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins - metabolism ; Nuclear Proteins - metabolism ; PC12 Cells ; Phosphotyrosine - metabolism ; Protein Binding ; Rats ; Sequence Homology, Amino Acid ; src Homology Domains</subject><ispartof>The Journal of biological chemistry, 1995-12, Vol.270 (52), p.30853-30856</ispartof><rights>1995 © 1995 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3</citedby><cites>FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8537337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fiore, Francesca</creatorcontrib><creatorcontrib>Zambrano, Nicola</creatorcontrib><creatorcontrib>Minopoli, Giuseppina</creatorcontrib><creatorcontrib>Donini, Virgilio</creatorcontrib><creatorcontrib>Duilio, Angela</creatorcontrib><creatorcontrib>Russo, Tommaso</creatorcontrib><title>The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two putative PID/PTB domains of Fe65 were used to construct glutathione S-transferase-Fe65 fusion proteins. Co-precipitation experiments demonstrated that the Fe65 PID/PTB domains interacted with several proteins of apparent molecular mass 135, 115, 105, and 51 kDa. The region of Fe65 containing the PID/PTB domains was used as a bait to screen a human brain cDNA library in yeast by the two-hybrid system. Three different cDNA clones were isolated, two of which contain overlapping segments of the cDNA encoding the COOH terminus of the Alzheimer's β-amyloid-precursor protein (APP), that represents the short intracellular domain of this membrane protein. The third clone contains a cDNA fragment coding for the COOH terminus of the human counterpart of a mouse β-amyloid-like precursor protein. The alignment of the three APP encoding cDNA fragments found in the screening suggests that the region of APP involved in the binding is centered on the NPTY sequence, which is analogous to that present in the intracellular domains of the growth factor receptors interacting with the PID/PTB domain of Shc.</description><subject>Alzheimer Disease - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Animals</subject><subject>DNA, Complementary</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nuclear Proteins - metabolism</subject><subject>PC12 Cells</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Sequence Homology, Amino Acid</subject><subject>src Homology Domains</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNqFUctu1DAUtRBVGQp7NkheIKCLTG3HjjPshkIfUiUqKBI7y3GuJ66SeLCTVsMX8Af8EF_Cl9TzUIUqIbyx7PO4R_cg9IKSKSWSH11XZsokmQo2zUkp8kdoQkmZZ7mg3x6jCSGMZjMmyifoaYzXJB0-o_toP1FlnssJ-n3VAP4MC-f7iL3FQ3qeQCHwZfADuB6f-c63fuHHiAe_gS8bH5eNH1bBR9cDPu8HCNoMyeLoIfbe9bXrF_iD73QySwO-NGbzu7FK0qSEth1bHf4irbF5-6MB10F4E_G8W7Xe1SkUmDFEH-7jvf3z89fhM7RndRvh-e4-QF9PPl4dn2UXn07Pj-cXmeFcDllecVMUlrOi4paVAqyZ6ZoT0IW2vBRGMCullmCosBZACAulKHlVWWm0NfkBer31XQb_fYQ4qM7FdXzdQ1qQklKWgvLiv0QqCeOUyUQkW6JJC4sBrFoG1-mwUpSodcMqNaxSw0owtWk4SV7uvMeqg_pesKs04a-2eOMWza0LoCrnTQPdQ5t3Wxqkhd04CCoaB72BOknMoGrv_p3hDvjmxpk</recordid><startdate>19951229</startdate><enddate>19951229</enddate><creator>Fiore, Francesca</creator><creator>Zambrano, Nicola</creator><creator>Minopoli, Giuseppina</creator><creator>Donini, Virgilio</creator><creator>Duilio, Angela</creator><creator>Russo, Tommaso</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19951229</creationdate><title>The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)</title><author>Fiore, Francesca ; Zambrano, Nicola ; Minopoli, Giuseppina ; Donini, Virgilio ; Duilio, Angela ; Russo, Tommaso</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Animals</topic><topic>DNA, Complementary</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nuclear Proteins - metabolism</topic><topic>PC12 Cells</topic><topic>Phosphotyrosine - metabolism</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Sequence Homology, Amino Acid</topic><topic>src Homology Domains</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fiore, Francesca</creatorcontrib><creatorcontrib>Zambrano, Nicola</creatorcontrib><creatorcontrib>Minopoli, Giuseppina</creatorcontrib><creatorcontrib>Donini, Virgilio</creatorcontrib><creatorcontrib>Duilio, Angela</creatorcontrib><creatorcontrib>Russo, Tommaso</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>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fiore, Francesca</au><au>Zambrano, Nicola</au><au>Minopoli, Giuseppina</au><au>Donini, Virgilio</au><au>Duilio, Angela</au><au>Russo, Tommaso</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-12-29</date><risdate>1995</risdate><volume>270</volume><issue>52</issue><spage>30853</spage><epage>30856</epage><pages>30853-30856</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Article-1</notes><notes>ObjectType-Feature-2</notes><abstract>Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two putative PID/PTB domains of Fe65 were used to construct glutathione S-transferase-Fe65 fusion proteins. Co-precipitation experiments demonstrated that the Fe65 PID/PTB domains interacted with several proteins of apparent molecular mass 135, 115, 105, and 51 kDa. The region of Fe65 containing the PID/PTB domains was used as a bait to screen a human brain cDNA library in yeast by the two-hybrid system. Three different cDNA clones were isolated, two of which contain overlapping segments of the cDNA encoding the COOH terminus of the Alzheimer's β-amyloid-precursor protein (APP), that represents the short intracellular domain of this membrane protein. The third clone contains a cDNA fragment coding for the COOH terminus of the human counterpart of a mouse β-amyloid-like precursor protein. The alignment of the three APP encoding cDNA fragments found in the screening suggests that the region of APP involved in the binding is centered on the NPTY sequence, which is analogous to that present in the intracellular domains of the growth factor receptors interacting with the PID/PTB domain of Shc.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8537337</pmid><doi>10.1074/jbc.270.52.30853</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1995-12, Vol.270 (52), p.30853-30856
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_77785146
source BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS
subjects Alzheimer Disease - metabolism
Amino Acid Sequence
Amyloid beta-Protein Precursor - metabolism
Animals
DNA, Complementary
Humans
Mice
Molecular Sequence Data
Nerve Tissue Proteins - metabolism
Nuclear Proteins - metabolism
PC12 Cells
Phosphotyrosine - metabolism
Protein Binding
Rats
Sequence Homology, Amino Acid
src Homology Domains
title The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (∗)
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-22T01%3A54%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Regions%20of%20the%20Fe65%20Protein%20Homologous%20to%20the%20Phosphotyrosine%20Interaction/Phosphotyrosine%20Binding%20Domain%20of%20Shc%20Bind%20the%20Intracellular%20Domain%20of%20the%20Alzheimer's%20Amyloid%20Precursor%20Protein%20(%E2%88%97)&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Fiore,%20Francesca&rft.date=1995-12-29&rft.volume=270&rft.issue=52&rft.spage=30853&rft.epage=30856&rft.pages=30853-30856&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.270.52.30853&rft_dat=%3Cproquest_cross%3E17024127%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c447t-3b4c66f426b4f285efc9ad40ea6af485c52f77a7ec15ffee55fe8584bbf7cafc3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=17024127&rft_id=info:pmid/8537337&rfr_iscdi=true