Nucleocytoplasmic shuttling of valosin-containing protein (VCP/p97) regulated by its N domain and C-terminal region

Changcheng Song; Qing Wang; Changzheng Song; Stephen J. Lockett; Nancy H. Colburn; Chou Chi H. Li; Ji Ming Wang; Thomas J. Rogers

doi:10.1016/j.bbamcr.2014.10.019

Nucleocytoplasmic shuttling of valosin-containing protein (VCP/p97) regulated by its N domain and C-terminal region

Changcheng Song
, Qing Wang
, Changzheng Song
, Stephen J. Lockett
, Nancy H. Colburn
, Chou Chi H. Li
, Ji Ming Wang
, Thomas J. Rogers

Producción científica: Article › revisión exhaustiva

16 Citas (Scopus)

Resumen

Valosin-containing protein (VCP or p97), a member of the AAA family (ATPases associated with diverse cellular activities), plays a key role in many important cellular activities. A genetic deficiency of VCP can cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD). Previous studies showed that the VCP N domain is essential for the regulation of nuclear entry of VCP. Here we report that IBMPFD mutations, which are mainly located in the N domain, suppress the nuclear entry of VCP. Moreover, the peptide sequence G₇₈₀AGPSQ in the C-terminal region regulates the retention of VCP in the nucleus. A mutant lacking this sequence can increase the nuclear distribution of IBMPFD VCP, suggesting that this sequence is a potential molecular target for correcting the deficient nucleocytoplasmic shuttling of IBMPFD VCP proteins.

Idioma original	English
Páginas (desde-hasta)	222-232
Número de páginas	11
Publicación	Biochimica et Biophysica Acta - Molecular Cell Research
Volumen	1853
N.º	1
DOI	https://doi.org/10.1016/j.bbamcr.2014.10.019
Estado	Published - ene 1 2015

Nota bibliográfica

Publisher Copyright:
© 2014 Elsevier B.V.

Financiación

We thank Drs. Carlos Barrero, Ying Wang and Ren-Ming Dai for technical support, and Dr. Madesh Muniswamy for providing the confocal imaging facility. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services nor does mention of trade names, commercial products, or organizations imply endorsement by the US Government. The publisher or recipient acknowledges the right of the US Government to retain a nonexclusive, royalty-free license in and to any copyright covering the manuscript. This research was funded by NIEHS 1R21ES023051 for C.S. Other supports include: DA-14230, DA-25532, and DA-13429 for T.J.R.; NCI Contract Nos. NO1CO56000 and HHSN261200800001E for S.L.; Intramural Research Program of the NIH National Cancer Institute Center for Cancer Research under contract N01-CO-12400 for N.C., C.C.L. and J.M.W.; National Natural Science Foundation of China Nos. 30672433 and 30271215 and Natural Science Foundation of Shandong Province No. 1872010ZRE27212 for S.C.Z.

Financiadores	Número del financiador
National Institutes of Health (NIH)	P01DA023860
National Childhood Cancer Registry – National Cancer Institute	HHSN261200800001E, N01-CO-12400, ZIABC010725, NO1CO56000
National Institutes of Health/National Institute of Environmental Health Sciences	R21ES023051, R01DA014230, P30DA013429, R01DA025532
National Natural Science Foundation of China (NSFC)	30271215, 30672433
Natural Science Foundation of Shandong Province	1872010ZRE27212

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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@article{c759ebc85c2b4a2785d1a4f549fe45f3,

title = "Nucleocytoplasmic shuttling of valosin-containing protein (VCP/p97) regulated by its N domain and C-terminal region",

abstract = "Valosin-containing protein (VCP or p97), a member of the AAA family (ATPases associated with diverse cellular activities), plays a key role in many important cellular activities. A genetic deficiency of VCP can cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD). Previous studies showed that the VCP N domain is essential for the regulation of nuclear entry of VCP. Here we report that IBMPFD mutations, which are mainly located in the N domain, suppress the nuclear entry of VCP. Moreover, the peptide sequence G780AGPSQ in the C-terminal region regulates the retention of VCP in the nucleus. A mutant lacking this sequence can increase the nuclear distribution of IBMPFD VCP, suggesting that this sequence is a potential molecular target for correcting the deficient nucleocytoplasmic shuttling of IBMPFD VCP proteins.",

keywords = "Inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD), Nuclear export signal, Nucleocytoplasmic shuttling, Valosin containing protein",

author = "Changcheng Song and Qing Wang and Changzheng Song and Lockett, \{Stephen J.\} and Colburn, \{Nancy H.\} and Li, \{Chou Chi H.\} and Wang, \{Ji Ming\} and Rogers, \{Thomas J.\}",

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doi = "10.1016/j.bbamcr.2014.10.019",

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AU - Song, Changcheng

AU - Wang, Qing

AU - Song, Changzheng

AU - Lockett, Stephen J.

AU - Colburn, Nancy H.

AU - Li, Chou Chi H.

AU - Wang, Ji Ming

AU - Rogers, Thomas J.

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Valosin-containing protein (VCP or p97), a member of the AAA family (ATPases associated with diverse cellular activities), plays a key role in many important cellular activities. A genetic deficiency of VCP can cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD). Previous studies showed that the VCP N domain is essential for the regulation of nuclear entry of VCP. Here we report that IBMPFD mutations, which are mainly located in the N domain, suppress the nuclear entry of VCP. Moreover, the peptide sequence G780AGPSQ in the C-terminal region regulates the retention of VCP in the nucleus. A mutant lacking this sequence can increase the nuclear distribution of IBMPFD VCP, suggesting that this sequence is a potential molecular target for correcting the deficient nucleocytoplasmic shuttling of IBMPFD VCP proteins.

AB - Valosin-containing protein (VCP or p97), a member of the AAA family (ATPases associated with diverse cellular activities), plays a key role in many important cellular activities. A genetic deficiency of VCP can cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD). Previous studies showed that the VCP N domain is essential for the regulation of nuclear entry of VCP. Here we report that IBMPFD mutations, which are mainly located in the N domain, suppress the nuclear entry of VCP. Moreover, the peptide sequence G780AGPSQ in the C-terminal region regulates the retention of VCP in the nucleus. A mutant lacking this sequence can increase the nuclear distribution of IBMPFD VCP, suggesting that this sequence is a potential molecular target for correcting the deficient nucleocytoplasmic shuttling of IBMPFD VCP proteins.

KW - Inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD)

KW - Nuclear export signal

KW - Nucleocytoplasmic shuttling

KW - Valosin containing protein

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JO - Biochimica et Biophysica Acta - Molecular Cell Research

JF - Biochimica et Biophysica Acta - Molecular Cell Research

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Nucleocytoplasmic shuttling of valosin-containing protein (VCP/p97) regulated by its N domain and C-terminal region

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ASJC Scopus subject areas

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