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ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain

หน่วยงาน Nanyang Technological University, Singapore

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ชื่อเรื่อง : ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain
นักวิจัย : Chia, Wei Sheng , Chia, Diana Xueqi , Rao, Feng , Nun, Shoshana Bar , Shochat, Susana Geifman
คำค้น : DRNTU::Science::Biological sciences
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2555
อ้างอิง : Chia, W. S., Chia, D. X., Rao, F., Nun, S. B., & Shochat, S. G. (2012). ATP Binding to p97/VCP D1 Domain Regulates Selective Recruitment of Adaptors to Its Proximal N-Domain. PLoS ONE, 7(12), e50490. , 1932-6203 , http://hdl.handle.net/10220/10921 , http://dx.doi.org/10.1371/journal.pone.0050490
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : PLoS ONE
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

p97/Valosin-containing protein (VCP) is a member of the AAA-ATPase family involved in many cellular processes including cell division, intracellular trafficking and extraction of misfolded proteins in endoplasmic reticulum-associated degradation (ERAD). It is a homohexamer with each subunit containing two tandem D1 and D2 ATPase domains and N- and C-terminal regions that function as adaptor protein binding domains. p97/VCP is directed to its many different functional pathways by associating with various adaptor proteins. The regulation of the recruitment of the adaptor proteins remains unclear. Two adaptor proteins, Ufd1/Npl4 and p47, which bind exclusively to the p97/VCP N-domain and direct p97/VCP to either ERAD-related processes or homotypic fusion of Golgi fragments, were studied here. Surface plasmon resonance biosensor-based assays allowed the study of binding kinetics in real time. In competition experiments, it was observed that in the presence of ATP, Ufd1/Npl4 was able to compete more effectively with p47 for binding to p97/VCP. By using non-hydrolysable ATP analogues and the hexameric truncated p97/N-D1 fragment, it was shown that binding rather than hydrolysis of ATP to the proximal D1 domain strengthened the Ufd1/Npl4 association with the N-domain, thus regulating the recruitment of either Ufd1/Npl4 or p47. This novel role of ATP and an assigned function to the D1 AAA-ATPase domain link the multiple functions of p97/VCP to the metabolic status of the cell.

บรรณานุกรม :
Chia, Wei Sheng , Chia, Diana Xueqi , Rao, Feng , Nun, Shoshana Bar , Shochat, Susana Geifman . (2555). ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Chia, Wei Sheng , Chia, Diana Xueqi , Rao, Feng , Nun, Shoshana Bar , Shochat, Susana Geifman . 2555. "ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Chia, Wei Sheng , Chia, Diana Xueqi , Rao, Feng , Nun, Shoshana Bar , Shochat, Susana Geifman . "ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2555. Print.
Chia, Wei Sheng , Chia, Diana Xueqi , Rao, Feng , Nun, Shoshana Bar , Shochat, Susana Geifman . ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2555.