Email updates

Keep up to date with the latest news and content from BMC Evolutionary Biology and BioMed Central.

Open Access Open Badges Research article

Molecular evolution of a-kinase anchoring protein (AKAP)-7: implications in comparative PKA compartmentalization

Keven R Johnson1, Jessie Nicodemus-Johnson2, Graeme K Carnegie3 and Robert S Danziger145*

Author Affiliations

1 Department of Medicine, University of Illinois at Chicago, Chicago, IL, USA

2 Department of Human Genetics, University of Chicago, Chicago, IL, USA

3 Department of Pharmacology, University of Illinois at Chicago, Chicago, IL, USA

4 Jesse Brown VA Medical Center, Chicago, IL, USA

5 Department of Cardiology, University of Illinois at Chicago, 840S. Wood Street, Chicago, IL 60612, USA

For all author emails, please log on.

BMC Evolutionary Biology 2012, 12:125  doi:10.1186/1471-2148-12-125

Published: 26 July 2012

Additional files

Additional file 1:

Figure S1. AKAP7 Splice Variant Evolution. EST classification and EST to gene matching shows the differential incorporation of AKAP7 splice variants throughout evolution. A cladogram was constructed using the NCBI taxonomy common tree tool and matches known species phylogenetic relationships. The accession numbers from NCBI or Ensemble databases and corresponding exon-intron structures in each species (determined by EST to gene matching) for the AKAP7 splice variants is shown in each column. A splice variant is indicated as “not present” if the exon(s) for that splice variant are absent from the AKAP7 gene. A splice variant is indicated as “not detected” if the necessary exons are identified in the AKAP7 gene but no EST was identified. Splice variants with a non-orthologous AKAP7γ exon-1 are listed as AKAP7γ-like.

Format: EPS Size: 352KB Download file

Open Data

Additional file 2:

Figure S2. Nucleotide and Amino acid alignments of human, mouse and rat AKAP7δ. (A) Human and mouse AKAP7δ splice variants were sequenced and aligned to the previously reported rat AKAP7δ nucleotide sequence. Predicted mutations in the AKAP7γ initiation codon are confirmed, and indicated by an (*). There is 78-89 % sequence identity between rat, mouse, and human AKAP7δ nucleotide sequence. The least similar region is found between nucleotides 180 and 200, (B) translated amino acid sequences were aligned using ClustalX2. Rat and mouse AKAP7δ contain an “RGD” domain between amino acids 70 and 75, this domain is absent from the human sequence.

Format: EPS Size: 4.4MB Download file

Open Data

Additional file 3:

Figure S3. Splice variants of Rat AKAP7δ. (A) PCR amplification of AKAP7δ from rat heart cDNA yielded two smaller splice variants in addition to the native form. (B) Rat AKAP7δ variant-1 has an exon-7 deletion, whereas AKAP7δ variant-2 consists of exons 1, 2 and 8, while exons 3–7 are deleted. Rat AKAP7δ variant-1 contains the AKAP7 NLS (dotted underline) but not the AKAP7 RI/RII binding domain. Rat AKAP7δ variant-2 lacks the AKAP7 NLS but contains the AKAP7 RI/RII binding domain (box).

Format: EPS Size: 93KB Download file

Open Data

Additional file 4:

Figure S4. Mouse AKAP7γ splice variant. A short splice variant consisting of AKAP7γ exons 1 and 2, and a unique 3’ exon was identified in mouse ESTs. (A) This truncated splice variant contains the AKAP7 NLS (dotted box), but lacks the AKAP7 RI/RII binding domain. A model was constructed (B) to show the relative positions of constituent exons. (C) The mouse AKAP7γ short variant is not widely expressed, and is detected only in the spleen.

Format: EPS Size: 110KB Download file

Open Data

Additional file 5:

Figure S5. Nucleotide and amino acid alignments of AKAP7 short form splice variants. (A) The amino terminus of AKAP7α and AKAP7β was aligned using clustalX2. Amino acid sequences are highly conserved from zebrafish to humans. Residues that have been previously identified as lipid-modified [1] are indicated by (‡) and hydrophobic residues are indicated with down-arrows (↓). (B) The AKAP7β-specific region is identified in species from pig to humans, with several highly conserved residues which are indicated with (*).

Format: EPS Size: 893KB Download file

Open Data