PubMed:10369872 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":0,"end":11},"obj":"protein"},{"id":"T2","span":{"begin":26,"end":31},"obj":"protein"},{"id":"T3","span":{"begin":35,"end":47},"obj":"protein"},{"id":"T4","span":{"begin":99,"end":111},"obj":"protein"},{"id":"T5","span":{"begin":113,"end":116},"obj":"protein"},{"id":"T6","span":{"begin":216,"end":227},"obj":"protein"},{"id":"T7","span":{"begin":229,"end":232},"obj":"protein"},{"id":"T8","span":{"begin":587,"end":590},"obj":"protein"},{"id":"T9","span":{"begin":594,"end":597},"obj":"protein"},{"id":"T10","span":{"begin":619,"end":624},"obj":"protein"},{"id":"T11","span":{"begin":628,"end":640},"obj":"protein"},{"id":"T12","span":{"begin":658,"end":681},"obj":"protein"},{"id":"T13","span":{"begin":737,"end":740},"obj":"protein"},{"id":"T14","span":{"begin":767,"end":772},"obj":"protein"},{"id":"T15","span":{"begin":855,"end":858},"obj":"protein"},{"id":"T16","span":{"begin":905,"end":907},"obj":"protein"},{"id":"T17","span":{"begin":908,"end":913},"obj":"protein"},{"id":"T18","span":{"begin":941,"end":944},"obj":"protein"}],"text":"Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport.\nPresenilin 1 (PS1) mutations account for the majority of early-onset dominant cases of familial Alzheimer's disease. Presenilins (PSs) are located in many intra-cellular compartments such as the endoplasmic reticulum, Golgi apparatus, nuclear region and vesicular structures. These proteins include from seven to nine putative transmembrane domains, with the N- and C-terminal ends and a large hydrophilic loop orientated towards the cytoplasm. We report an interaction between the human PS1 or PS2 hydrophilic loop and Rab11, a small GTPase belonging to the Ras-related superfamily. Interaction domains were mapped to codons 374-400 for PS1 and to codons 106-179 for Rab11, a region including the fourth GTP-binding domain. Considering the implication of Rab proteins in vesicular transport pathways, the PS-Rab11 inter-action suggests that PSs might be involved in amyloid precursor protein vesicular routing."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":26,"end":31},"obj":"protein"},{"id":"T2","span":{"begin":100,"end":111},"obj":"protein"},{"id":"T3","span":{"begin":113,"end":116},"obj":"protein"},{"id":"T4","span":{"begin":587,"end":590},"obj":"protein"},{"id":"T5","span":{"begin":594,"end":597},"obj":"protein"},{"id":"T6","span":{"begin":619,"end":624},"obj":"protein"},{"id":"T7","span":{"begin":737,"end":740},"obj":"protein"},{"id":"T8","span":{"begin":767,"end":772},"obj":"protein"},{"id":"T9","span":{"begin":908,"end":913},"obj":"protein"}],"text":"Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport.\nPresenilin 1 (PS1) mutations account for the majority of early-onset dominant cases of familial Alzheimer's disease. Presenilins (PSs) are located in many intra-cellular compartments such as the endoplasmic reticulum, Golgi apparatus, nuclear region and vesicular structures. These proteins include from seven to nine putative transmembrane domains, with the N- and C-terminal ends and a large hydrophilic loop orientated towards the cytoplasm. We report an interaction between the human PS1 or PS2 hydrophilic loop and Rab11, a small GTPase belonging to the Ras-related superfamily. Interaction domains were mapped to codons 374-400 for PS1 and to codons 106-179 for Rab11, a region including the fourth GTP-binding domain. Considering the implication of Rab proteins in vesicular transport pathways, the PS-Rab11 inter-action suggests that PSs might be involved in amyloid precursor protein vesicular routing."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":195,"end":214},"obj":"HP_0002511"},{"id":"T2","span":{"begin":966,"end":973},"obj":"HP_0011034"}],"text":"Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport.\nPresenilin 1 (PS1) mutations account for the majority of early-onset dominant cases of familial Alzheimer's disease. Presenilins (PSs) are located in many intra-cellular compartments such as the endoplasmic reticulum, Golgi apparatus, nuclear region and vesicular structures. These proteins include from seven to nine putative transmembrane domains, with the N- and C-terminal ends and a large hydrophilic loop orientated towards the cytoplasm. We report an interaction between the human PS1 or PS2 hydrophilic loop and Rab11, a small GTPase belonging to the Ras-related superfamily. Interaction domains were mapped to codons 374-400 for PS1 and to codons 106-179 for Rab11, a region including the fourth GTP-binding domain. Considering the implication of Rab proteins in vesicular transport pathways, the PS-Rab11 inter-action suggests that PSs might be involved in amyloid precursor protein vesicular routing."}