The University of Southampton
University of Southampton Institutional Repository

Centriolar association of ALMS1 and likely centrosomal functions of the ALMS motif-containing proteins C10orf90 and KIAA1731

Centriolar association of ALMS1 and likely centrosomal functions of the ALMS motif-containing proteins C10orf90 and KIAA1731
Centriolar association of ALMS1 and likely centrosomal functions of the ALMS motif-containing proteins C10orf90 and KIAA1731
Mutations in the human gene ALMS1 cause Alström syndrome, a rare progressive condition characterized by neurosensory degeneration and metabolic defects. ALMS1 protein localizes to the centrosome and has been implicated in the assembly and/or maintenance of primary cilia, however its precise function, distribution within the centrosome and mechanism of centrosomal recruitment are unknown. The C-terminus of ALMS1 contains a region with similarity to the uncharacterized human protein C10orf90, termed the ALMS motif. Here, we show that a third human protein, the candidate centrosomal protein KIAA1731, contains an ALMS motif, and that exogenously expressed KIAA1731 and C10orf90 localize to the centrosome. However, based on deletion analysis of ALMS1, the ALMS motif appears unlikely to be critical for centrosomal-targeting. RNAi analyses suggest that C10orf90 and KIAA1731 have roles in primary cilium assembly and centriole formation/stability respectively. We also show that ALMS1 localizes specifically to the proximal ends of centrioles and basal bodies, where it colocalizes with the centrosome cohesion protein C-Nap1. RNAi analysis reveals markedly diminished centrosomal levels of C-Nap1 and compromised cohesion of parental centrioles in ALMS1-depleted cells. In summary, these data suggest centrosomal functions for C10orf90 and KIAA1731 and new centriole-related functions for ALMS1.

1059-1524
3617-3629
Knorz, Victoria J.
f0084ead-54c9-4885-b60e-9360dcf3d524
Spalluto, Cosma
6802ad50-bc38-404f-9a19-40916425183b
Lessard, Mark
697b65de-ba8e-4bba-a158-28a003558229
Purvis, Tracey L.
a2941cc1-e316-42ea-a24a-c6395b701ec6
Adigun, Fiona F.
2269c4d5-9c91-43fb-a0d7-8a07a24c0b76
Collin, Gayle B.
1363ff94-ef41-4119-b355-ec4bf6f177fc
Hanley, Neil A.
bf03f7bb-f377-44fb-8344-0bb1ca8b2ef9
Wilson, David I.
1500fca1-7082-4271-95f4-691f1d1252a2
Hearn, Thomas
6426d3f3-0083-4c1c-a604-1319878b3363
Knorz, Victoria J.
f0084ead-54c9-4885-b60e-9360dcf3d524
Spalluto, Cosma
6802ad50-bc38-404f-9a19-40916425183b
Lessard, Mark
697b65de-ba8e-4bba-a158-28a003558229
Purvis, Tracey L.
a2941cc1-e316-42ea-a24a-c6395b701ec6
Adigun, Fiona F.
2269c4d5-9c91-43fb-a0d7-8a07a24c0b76
Collin, Gayle B.
1363ff94-ef41-4119-b355-ec4bf6f177fc
Hanley, Neil A.
bf03f7bb-f377-44fb-8344-0bb1ca8b2ef9
Wilson, David I.
1500fca1-7082-4271-95f4-691f1d1252a2
Hearn, Thomas
6426d3f3-0083-4c1c-a604-1319878b3363

Knorz, Victoria J., Spalluto, Cosma, Lessard, Mark, Purvis, Tracey L., Adigun, Fiona F., Collin, Gayle B., Hanley, Neil A., Wilson, David I. and Hearn, Thomas (2010) Centriolar association of ALMS1 and likely centrosomal functions of the ALMS motif-containing proteins C10orf90 and KIAA1731. Molecular Biology of the Cell, 21 (12), 3617-3629. (doi:10.1091/mbc.E10-03-0246). (PMID:20844083)

Record type: Article

Abstract

Mutations in the human gene ALMS1 cause Alström syndrome, a rare progressive condition characterized by neurosensory degeneration and metabolic defects. ALMS1 protein localizes to the centrosome and has been implicated in the assembly and/or maintenance of primary cilia, however its precise function, distribution within the centrosome and mechanism of centrosomal recruitment are unknown. The C-terminus of ALMS1 contains a region with similarity to the uncharacterized human protein C10orf90, termed the ALMS motif. Here, we show that a third human protein, the candidate centrosomal protein KIAA1731, contains an ALMS motif, and that exogenously expressed KIAA1731 and C10orf90 localize to the centrosome. However, based on deletion analysis of ALMS1, the ALMS motif appears unlikely to be critical for centrosomal-targeting. RNAi analyses suggest that C10orf90 and KIAA1731 have roles in primary cilium assembly and centriole formation/stability respectively. We also show that ALMS1 localizes specifically to the proximal ends of centrioles and basal bodies, where it colocalizes with the centrosome cohesion protein C-Nap1. RNAi analysis reveals markedly diminished centrosomal levels of C-Nap1 and compromised cohesion of parental centrioles in ALMS1-depleted cells. In summary, these data suggest centrosomal functions for C10orf90 and KIAA1731 and new centriole-related functions for ALMS1.

This record has no associated files available for download.

More information

Published date: November 2010
Organisations: Human Genetics

Identifiers

Local EPrints ID: 164177
URI: http://eprints.soton.ac.uk/id/eprint/164177
ISSN: 1059-1524
PURE UUID: 7dedd94c-4eb1-4f8e-9f85-57c7e428e307
ORCID for Cosma Spalluto: ORCID iD orcid.org/0000-0001-7273-0844
ORCID for Thomas Hearn: ORCID iD orcid.org/0000-0002-8670-6236

Catalogue record

Date deposited: 05 Oct 2010 11:57
Last modified: 14 Mar 2024 02:46

Export record

Altmetrics

Contributors

Author: Victoria J. Knorz
Author: Cosma Spalluto ORCID iD
Author: Mark Lessard
Author: Tracey L. Purvis
Author: Fiona F. Adigun
Author: Gayle B. Collin
Author: Neil A. Hanley
Author: David I. Wilson
Author: Thomas Hearn ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×