A Proteomic Analysis of Human Cilia

Ostrowski, Lawrence E.; Blackburn, Kevin; Radde, Kristen M.; Moyer, Mary B.; Schlatzer, Daniela; Moseley, Arthur; Boucher, Richard C.

doi:10.1074/mcp.m200037-mcp200

Cited by 406 publications

(155 citation statements)

References 31 publications

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“…The general lysis and extraction procedure used has the advantage that it provides a general idea of the types of proteins that constitute the sperm proteome. Therefore, this approach should be complementary to other proteomic approaches focusing on specific compartments or organelles such as the cytoplasm, membrane, cytoskeleton, tail, acrosome or sperm head [8][9][10][11][24][25][26][27][28].…”

Section: Resultsmentioning

confidence: 99%

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Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

230

177

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Conventional 1-DE has in the past provided a wealth of information concerning the major sperm proteins. However, so far there are relatively few reports exploiting the potential of the present proteomic tools to identify and to study additional yet-unidentified important proteins present in human spermatozoa. In the present work, 2-DE of proteins extracted from human normozoospermic spermatozoa led to the resolution of over 1000 spots. Subsequent excision from the gels of 145 spots and MALDI-TOF MS analysis allowed the identification of 98 different proteins. The function of these proteins turned out to be energy production (23%), transcription, protein synthesis, transport, folding and turnover (23%), cell cycle, apoptosis and oxidative stress (10%), signal transduction (8%), cytoskeleton, flagella and cell movement (10%), cell recognition (7%), metabolism (6%) and unknown function (11%). As many as 23% of the proteins identified have not been previously described as being expressed in human spermatozoa. The present data provide an important clue towards determining the function of these proteins and opens up the possibility to perform additional experiments.

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Section: Resultsmentioning

confidence: 99%

“…In man, specific approaches to target subcellular organelles or compartments have been successfully used [11,[24][25][26][27][28]. A 2-D protein map of the human sperm head has been described, but without MS identification [29].…”

Section: Introductionmentioning

confidence: 99%

Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

230

177

View full text Add to dashboard Cite

show abstract

“…Eukaryotic axonemes are made of 200-400 proteins, few of which have been identified or functionally characterized [30][31][32]. All sperm that have been studied require cAMP dependent protein kinase (PKA) phosphorylation to initiate and maintain flagellar motility [30,33].…”

Section: Susac Associated Proteinsmentioning

confidence: 99%

A soluble adenylyl cyclase from sea urchin spermatozoa

Nomura

Beltrán

Darszon

et al. 2005

Gene

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“…Through proteomic analysis of human bronchial epithelial cells and immunofluorescence staining of mouse tracheal epithelial cells, RSP3 has been found in motile cilia in mammals (16,17). Mammals contain one RSP3 gene (mapped to chromosomal locus 6q25.3), composed of eight exons and seven introns.…”

mentioning

confidence: 99%

Radial Spoke Protein 3 Is a Mammalian Protein Kinase A-anchoring Protein That Binds ERK1/2

Jivan¹,

Earnest

Juang

et al. 2009

Journal of Biological Chemistry

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Initially identified in Chlamydomonas, RSP3 (radial spoke protein 3) is 1 of more than 20 identified radial spoke structural components of motile cilia and is required for axonemal sliding and flagellar motility. The mammalian orthologs for this and other radial spoke proteins, however, remain to be characterized. We found mammalian RSP3 to bind to the MAPK ERK2 through a yeast two-hybrid screen designed to identify interacting proteins that have a higher affinity for the phosphorylated, active form of the protein kinase. Consistent with the screening result, the human homolog, RSPH3, interacts with and is a substrate for ERK1/2. Moreover, RSPH3 is a protein kinase A-anchoring protein (AKAP) that scaffolds the cAMP-dependent protein kinase holoenzyme. The binding of RSPH3 to the regulatory subunits of cAMP-dependent protein kinase, RII␣ and RII␤, is regulated by ERK1/2 activity and phosphorylation. Here we describe an ERK1/2-interacting AKAP and suggest a mechanism by which cAMP-dependent protein kinase-AKAP binding can be modulated by the activity of other enzymes.

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A Proteomic Analysis of Human Cilia

Cited by 406 publications

References 31 publications

Proteomic identification of human sperm proteins

Proteomic identification of human sperm proteins

A soluble adenylyl cyclase from sea urchin spermatozoa

Radial Spoke Protein 3 Is a Mammalian Protein Kinase A-anchoring Protein That Binds ERK1/2

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