Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0002686
Title: Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons
Authors: Buschdorf, J.P.
Chew, L.L. 
Soh, U.J.K. 
Liou Yih-Cherng, Y.-C. 
Low, B.C. 
Issue Date: 16-Jul-2008
Citation: Buschdorf, J.P., Chew, L.L., Soh, U.J.K., Liou Yih-Cherng, Y.-C., Low, B.C. (2008-07-16). Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons. PLoS ONE 3 (7) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0002686
Abstract: Mutations in ATCAY that encodes the brain specific protein BNIP-H (or Caytaxin) lead to Cayman cerebellar ataxia. BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. BNIP H interacted with Pin1 after nerve growth factor stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Although these two sites do not contain any of the canonical Pin1-binding motifs they showed differential binding profiles to Pin1 WW domain mutants S16E, S16A and W34A, and the catalytically inert C113A of its isomerase domain. Furthermore, their direct interation would occur only upon disrupting the ability of BNIP-H to form an intramolecular interaction by two similar regions. Furthermore, expression of Pin1 disrupted the BNIP-H/ glutaminase complex formation PC12 cells under nerve growth factor simulation. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Such a mechanism could provide a post-translational regulation on the cellular activity of BNIP-H during neuronal differentiation. © 2008 Buschdorf et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/101191
ISSN: 19326203
DOI: 10.1371/journal.pone.0002686
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
2008-nerve_growth_factor_stimulates_interaction_Cayman-pub.pdf756.76 kBAdobe PDF

OPEN

PublishedView/Download

SCOPUSTM   
Citations

20
checked on Jul 18, 2019

WEB OF SCIENCETM
Citations

18
checked on Jul 1, 2019

Page view(s)

49
checked on Jul 20, 2019

Download(s)

2
checked on Jul 20, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.