PMID- 10319321
OWN - NLM
STAT- MEDLINE
DCOM- 19990708
LR  - 20071115
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 13
IP  - 5
DP  - 1999 May
TI  - Isolation and molecular characterization of AKAP110, a novel, sperm-specific
      protein kinase A-anchoring protein.
PG  - 705-17
AB  - Agents that increase intracellular cAMP are potent stimulators of sperm motility.
      Anchoring inhibitor peptides, designed to disrupt the interaction of the
      cAMP-dependent protein kinase A (PKA) with A kinase-anchoring proteins (AKAPs),
      are potent inhibitors of sperm motility. These data suggest that PKA anchoring is
      a key biochemical mechanism controlling motility. We now report the isolation,
      identification, cloning, and characterization of AKAP110, the predominant AKAP
      detected in sperm lysates. AKAP110 cDNA was isolated and sequenced from mouse,
      bovine, and human testis libraries. Using truncated mutants, the RII-binding
      domain was identified. Alignment of the RII-binding domain on AKAP110 to those
      from other AKAPs reveals that AKAPs contain eight functionally conserved
      positions within an amphipathic helix structure that are responsible for RII
      interaction. Northern analysis of eight different tissues detected AKAP110 only
      in the testis, and in situ hybridization analysis detected AKAP110 only in round 
      spermatids, suggesting that AKAP110 is a protein found only in male germ cells.
      Sperm cells contain both RI, located primarily in the acrosomal region of the
      head, and RII, located exclusively in the tail, regulatory subunits of PKA.
      Immunocytochemical analysis detected AKAP110 in the acrosomal region of the sperm
      head and along the entire length of the principal piece. These data suggest that 
      AKAP110 shares compartments with both RI and RII isoforms of PKA and may function
      as a regulator of both motility- and head-associated functions such as
      capacitation and the acrosome reaction.
FAU - Vijayaraghavan, S
AU  - Vijayaraghavan S
AD  - Kent State University, Ohio 44242, USA.
FAU - Liberty, G A
AU  - Liberty GA
FAU - Mohan, J
AU  - Mohan J
FAU - Winfrey, V P
AU  - Winfrey VP
FAU - Olson, G E
AU  - Olson GE
FAU - Carr, D W
AU  - Carr DW
LA  - eng
SI  - GENBANK/AF093406
SI  - GENBANK/AF093407
SI  - GENBANK/AF093408
GR  - HD-36408/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (A Kinase Anchor Proteins)
RN  - 0 (AKAP3 protein, human)
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Akap3 protein, mouse)
RN  - 0 (Carrier Proteins)
RN  - 0 (Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Seminal Plasma Proteins)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
SB  - IM
MH  - A Kinase Anchor Proteins
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Carrier Proteins/*genetics/*metabolism
MH  - Cattle
MH  - Cloning, Molecular
MH  - Cyclic AMP-Dependent Protein Kinases/metabolism
MH  - Humans
MH  - In Situ Hybridization
MH  - Male
MH  - Mice
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Proteins/*genetics/isolation & purification/*metabolism
MH  - RNA, Messenger/metabolism
MH  - *Seminal Plasma Proteins
MH  - Sequence Analysis
MH  - Sequence Homology, Amino Acid
MH  - Sperm Motility
MH  - Spermatozoa/*physiology
MH  - Subcellular Fractions
MH  - Testis/physiology
EDAT- 1999/05/13 00:00
MHDA- 1999/05/13 00:01
CRDT- 1999/05/13 00:00
PHST- 1999/05/13 00:00 [pubmed]
PHST- 1999/05/13 00:01 [medline]
PHST- 1999/05/13 00:00 [entrez]
AID - 10.1210/mend.13.5.0278 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1999 May;13(5):705-17. doi: 10.1210/mend.13.5.0278.