Linked Life Data

21240291

Source:http://linkedlifedata.com/resource/pubmed/id/21240291

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-3-8
pubmed:abstractText
Calcium-binding tyrosine phosphorylation-regulated protein (CABYR) is a highly polymorphic calcium-binding tyrosine- and serine-/threonine-phosphorylated fibrous sheath (FS) protein involved in capacitation. A putative domain (amino acids 12-48) homologous to the regulatory subunit of type II cAMP-dependent protein kinase A (RII) dimerisation and A kinase-anchoring protein (AKAP)-binding domains of protein kinase A at the N-terminus suggests that CABYR may self-assemble and bind to AKAPs. Moreover, there is evidence that CABYR has limited interaction with AKAPs. However, further evidence and new relationships between CABYR and other FS proteins, including AKAPs, will be helpful in understanding the basic physiology of FS. In this study, a new strategy for co-immunoprecipitation of insoluble proteins, as well as the standard co-immunoprecipitation method in combination with mass spectrometry and western blot, was employed to explore the relationship between CABYR, AKAP3 and Ropporin. The results showed that AKAP3 was co-immunoprecipitated with CABYR by the anti-CABYR-A polyclonal antibody, and, conversely, CABYR was also co-immunoprecipitated with AKAP3 by the anti-AKAP3 polyclonal antibody. Another RII-like domain containing protein, Ropporin, was also co-immunoprecipitated with CABYR, indicating that Ropporin is one of CABYR's binding partners. The interactions between CABYR, AKAP3 and Ropporin were confirmed by yeast two-hybrid assays. Further analysis showed that CABYR not only binds to AKAP3 by its RII domain but binds to Ropporin through other regions besides the RII-like domain. This is the first demonstration that CABYR variants form a complex not only with the scaffolding protein AKAP3 but also with another RII-like domain-containing protein in the human sperm FS.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1745-7262
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
266-74
pubmed:meshHeading
pubmed-meshheading:21240291-A Kinase Anchor Proteins, pubmed-meshheading:21240291-Amino Acid Sequence, pubmed-meshheading:21240291-Calcium-Binding Proteins, pubmed-meshheading:21240291-Genetic Variation, pubmed-meshheading:21240291-Humans, pubmed-meshheading:21240291-Immunoprecipitation, pubmed-meshheading:21240291-Male, pubmed-meshheading:21240291-Membrane Proteins, pubmed-meshheading:21240291-Molecular Sequence Data, pubmed-meshheading:21240291-Multiprotein Complexes, pubmed-meshheading:21240291-Phosphoproteins, pubmed-meshheading:21240291-Protein Binding, pubmed-meshheading:21240291-Protein Interaction Domains and Motifs, pubmed-meshheading:21240291-Recombinant Fusion Proteins, pubmed-meshheading:21240291-Sperm Tail, pubmed-meshheading:21240291-Two-Hybrid System Techniques, pubmed-meshheading:21240291-rho GTP-Binding Proteins
pubmed:year
2011
pubmed:articleTitle
CABYR binds to AKAP3 and Ropporin in the human sperm fibrous sheath.
pubmed:affiliation
Department of Urology, Daping Hospital, Institute of Surgery Research, Third Military Medical University, Chongqing 400042, China. lyf1000@yahoo.com.cn
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural