Identification of PLP2 and RAB5C as novel TPD52 binding partners through yeast two-hybrid screening

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• 作者：Hamideh Shahheydari (1) (2)
  Sarah Frost (1) (2)
  Brian J. Smith (3)
  Guy E. Groblewski (4)
  Yuyan Chen (1) (2)
  Jennifer A. Byrne (1) (2)
  
• 关键词：TPD52 ; Yeast two ; hybrid ; Pull down ; PLP2 ; RAB5
• 刊名：Molecular Biology Reports
• 出版年：2014
• 出版时间：July 2014
• 年：2014
• 卷：41
• 期：7
• 页码：4565-4572
• 全文大小：992 KB
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• 作者单位：Hamideh Shahheydari (1) (2)
  Sarah Frost (1) (2)
  Brian J. Smith (3)
  Guy E. Groblewski (4)
  Yuyan Chen (1) (2)
  Jennifer A. Byrne (1) (2)
  
  1. Children鈥檚 Cancer Research Unit, Kids Research Institute, The Children鈥檚 Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia
  2. The University of Sydney Discipline of Paediatrics and Child Health, The Children鈥檚 Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia
  3. Department of Chemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, 3086, Australia
  4. Department of Nutritional Sciences, University of Wisconsin-Madison, Madison, WI, USA
  
• ISSN：1573-4978

文摘

Tumor protein D52 (TPD52) is overexpressed in different cancers, but its molecular functions are poorly defined. A large, low-stringency yeast two-hybrid screen using full-length TPD52 bait identified known partners (TPD52, TPD52L1, TPD52L2, MAL2) and four other preys that reproducibly bound TPD52 and TPD52L1 baits (PLP2, RAB5C, GOLGA5, YIF1A). PLP2 and RAB5 interactions with TPD52 were confirmed in pull down assays, with interaction domain mapping experiments indicating that both proteins interact with a novel binding region of TPD52. This study provides insights into TPD52 functions, and ways to maximise the efficiency of low-stringency yeast two-hybrid screens.