Loss of ASP but not ROPN1 reduces mammalian ciliary motility

Sarah E. Fiedler, Joseph H. Sisson, Todd A. Wyatt, Jacqueline A. Pavlik, Todd M. Gambling, Johnny L. Carson, Daniel Carr

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Protein kinase A (PKA) signaling is targeted by interactions with A-kinase anchoring proteins (AKAPs) via a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins [AKAP-associated sperm protein (ASP), ropporin (ROPN1), sperm protein 17 (SP17) and calcium binding tyrosine-(Y)-phosphorylation regulated protein (CABYR)] share this highly conserved RII dimerization/docking (R2D2) domain. ASP and ROPN1 are 41% identical in sequence, interact with a variety of AKAPs in a manner similar to PKA, and are expressed in ciliated and flagellated human cells. To test the hypothesis that these proteins regulate motility, we developed mutant mouse lines lacking ASP or ROPN1. Both mutant lines produced normal numbers of cilia with intact ciliary ultrastructure. Lack of ROPN1 had no effect on ciliary motility. However, the beat frequency of cilia from mice lacking ASP is significantly slower than wild type, indicating that ASP signaling may regulate ciliary motility. This is the first demonstration of in vivo function for ASP. Similar localization of ASP in mice and humans indicates that these findings may translate to human physiology, and that these mice will be an excellent model for future studies related to the pathogenesis of human disease. Published 2011 Wiley Periodicals, Inc.

Original languageEnglish (US)
Pages (from-to)22-32
Number of pages11
JournalCytoskeleton
Volume69
Issue number1
DOIs
StatePublished - Jan 2012

Fingerprint

Spermatozoa
Proteins
Cyclic AMP-Dependent Protein Kinases
Protein Kinases
Cilia
Dimerization
Molecular Motor Proteins
Staphylococcal Protein A
Tyrosine
Phosphorylation
Calcium

Keywords

  • A-kinase anchoring protein
  • OmniBank®
  • ROPN1L
  • Ropporin

ASJC Scopus subject areas

  • Cell Biology
  • Structural Biology

Cite this

Fiedler, S. E., Sisson, J. H., Wyatt, T. A., Pavlik, J. A., Gambling, T. M., Carson, J. L., & Carr, D. (2012). Loss of ASP but not ROPN1 reduces mammalian ciliary motility. Cytoskeleton, 69(1), 22-32. https://doi.org/10.1002/cm.20539

Loss of ASP but not ROPN1 reduces mammalian ciliary motility. / Fiedler, Sarah E.; Sisson, Joseph H.; Wyatt, Todd A.; Pavlik, Jacqueline A.; Gambling, Todd M.; Carson, Johnny L.; Carr, Daniel.

In: Cytoskeleton, Vol. 69, No. 1, 01.2012, p. 22-32.

Research output: Contribution to journalArticle

Fiedler, SE, Sisson, JH, Wyatt, TA, Pavlik, JA, Gambling, TM, Carson, JL & Carr, D 2012, 'Loss of ASP but not ROPN1 reduces mammalian ciliary motility', Cytoskeleton, vol. 69, no. 1, pp. 22-32. https://doi.org/10.1002/cm.20539
Fiedler SE, Sisson JH, Wyatt TA, Pavlik JA, Gambling TM, Carson JL et al. Loss of ASP but not ROPN1 reduces mammalian ciliary motility. Cytoskeleton. 2012 Jan;69(1):22-32. https://doi.org/10.1002/cm.20539
Fiedler, Sarah E. ; Sisson, Joseph H. ; Wyatt, Todd A. ; Pavlik, Jacqueline A. ; Gambling, Todd M. ; Carson, Johnny L. ; Carr, Daniel. / Loss of ASP but not ROPN1 reduces mammalian ciliary motility. In: Cytoskeleton. 2012 ; Vol. 69, No. 1. pp. 22-32.
@article{d3bee28a1eaf4742912184cde0f55c02,
title = "Loss of ASP but not ROPN1 reduces mammalian ciliary motility",
abstract = "Protein kinase A (PKA) signaling is targeted by interactions with A-kinase anchoring proteins (AKAPs) via a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins [AKAP-associated sperm protein (ASP), ropporin (ROPN1), sperm protein 17 (SP17) and calcium binding tyrosine-(Y)-phosphorylation regulated protein (CABYR)] share this highly conserved RII dimerization/docking (R2D2) domain. ASP and ROPN1 are 41{\%} identical in sequence, interact with a variety of AKAPs in a manner similar to PKA, and are expressed in ciliated and flagellated human cells. To test the hypothesis that these proteins regulate motility, we developed mutant mouse lines lacking ASP or ROPN1. Both mutant lines produced normal numbers of cilia with intact ciliary ultrastructure. Lack of ROPN1 had no effect on ciliary motility. However, the beat frequency of cilia from mice lacking ASP is significantly slower than wild type, indicating that ASP signaling may regulate ciliary motility. This is the first demonstration of in vivo function for ASP. Similar localization of ASP in mice and humans indicates that these findings may translate to human physiology, and that these mice will be an excellent model for future studies related to the pathogenesis of human disease. Published 2011 Wiley Periodicals, Inc.",
keywords = "A-kinase anchoring protein, OmniBank{\circledR}, ROPN1L, Ropporin",
author = "Fiedler, {Sarah E.} and Sisson, {Joseph H.} and Wyatt, {Todd A.} and Pavlik, {Jacqueline A.} and Gambling, {Todd M.} and Carson, {Johnny L.} and Daniel Carr",
year = "2012",
month = "1",
doi = "10.1002/cm.20539",
language = "English (US)",
volume = "69",
pages = "22--32",
journal = "Cytoskeleton",
issn = "1949-3584",
publisher = "Wiley-Liss Inc.",
number = "1",

}

TY - JOUR

T1 - Loss of ASP but not ROPN1 reduces mammalian ciliary motility

AU - Fiedler, Sarah E.

AU - Sisson, Joseph H.

AU - Wyatt, Todd A.

AU - Pavlik, Jacqueline A.

AU - Gambling, Todd M.

AU - Carson, Johnny L.

AU - Carr, Daniel

PY - 2012/1

Y1 - 2012/1

N2 - Protein kinase A (PKA) signaling is targeted by interactions with A-kinase anchoring proteins (AKAPs) via a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins [AKAP-associated sperm protein (ASP), ropporin (ROPN1), sperm protein 17 (SP17) and calcium binding tyrosine-(Y)-phosphorylation regulated protein (CABYR)] share this highly conserved RII dimerization/docking (R2D2) domain. ASP and ROPN1 are 41% identical in sequence, interact with a variety of AKAPs in a manner similar to PKA, and are expressed in ciliated and flagellated human cells. To test the hypothesis that these proteins regulate motility, we developed mutant mouse lines lacking ASP or ROPN1. Both mutant lines produced normal numbers of cilia with intact ciliary ultrastructure. Lack of ROPN1 had no effect on ciliary motility. However, the beat frequency of cilia from mice lacking ASP is significantly slower than wild type, indicating that ASP signaling may regulate ciliary motility. This is the first demonstration of in vivo function for ASP. Similar localization of ASP in mice and humans indicates that these findings may translate to human physiology, and that these mice will be an excellent model for future studies related to the pathogenesis of human disease. Published 2011 Wiley Periodicals, Inc.

AB - Protein kinase A (PKA) signaling is targeted by interactions with A-kinase anchoring proteins (AKAPs) via a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins [AKAP-associated sperm protein (ASP), ropporin (ROPN1), sperm protein 17 (SP17) and calcium binding tyrosine-(Y)-phosphorylation regulated protein (CABYR)] share this highly conserved RII dimerization/docking (R2D2) domain. ASP and ROPN1 are 41% identical in sequence, interact with a variety of AKAPs in a manner similar to PKA, and are expressed in ciliated and flagellated human cells. To test the hypothesis that these proteins regulate motility, we developed mutant mouse lines lacking ASP or ROPN1. Both mutant lines produced normal numbers of cilia with intact ciliary ultrastructure. Lack of ROPN1 had no effect on ciliary motility. However, the beat frequency of cilia from mice lacking ASP is significantly slower than wild type, indicating that ASP signaling may regulate ciliary motility. This is the first demonstration of in vivo function for ASP. Similar localization of ASP in mice and humans indicates that these findings may translate to human physiology, and that these mice will be an excellent model for future studies related to the pathogenesis of human disease. Published 2011 Wiley Periodicals, Inc.

KW - A-kinase anchoring protein

KW - OmniBank®

KW - ROPN1L

KW - Ropporin

UR - http://www.scopus.com/inward/record.url?scp=84855920492&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84855920492&partnerID=8YFLogxK

U2 - 10.1002/cm.20539

DO - 10.1002/cm.20539

M3 - Article

C2 - 22021175

AN - SCOPUS:84855920492

VL - 69

SP - 22

EP - 32

JO - Cytoskeleton

JF - Cytoskeleton

SN - 1949-3584

IS - 1

ER -