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Gene Review

AKAP8L  -  A kinase (PRKA) anchor protein 8-like

Homo sapiens

Synonyms: A-kinase anchor protein 8-like, AKAP8-like protein, HA95, HAP95, HRIHFB2018, ...
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Disease relevance of AKAP8L


High impact information on AKAP8L

  • HDAC3 forms a complex with A-Kinase-Anchoring Proteins AKAP95 and HA95, which are targeted to mitotic chromosomes [4].
  • HA95-LAP2 beta interaction is not required for NE formation [5].
  • A second domain sufficient to bind HA95 colocalizes with the lamin B-binding domain of LAP2beta at residues 299-373 [5].
  • HA95 is a chromatin-associated protein that interfaces the nuclear envelope (NE) and chromatin [5].
  • We propose that an interaction of LAP2beta, or LAP2 proteins, with HA95 is involved in the control of initiation of DNA replication [5].

Biological context of AKAP8L


Anatomical context of AKAP8L

  • The data also suggest that HA95 is not involved in initial binding of membranes to chromatin upon nuclear reassembly [6].
  • Intra-nuclear blocking of HA95 with anti-HA95 antibodies abolishes nuclear breakdown in a mitotic HeLa cell extract [6].

Physical interactions of AKAP8L

  • Taken together, these data support the proposal that HAP95 specifically facilitates CTE-mediated gene expression by directly binding to RHA [1].

Co-localisations of AKAP8L


Regulatory relationships of AKAP8L

  • Inhibition of PKC, MAP kinase, or CaM kinase II does not affect mitotic extract-induced dissociation of LAP2beta from HA95 [8].

Other interactions of AKAP8L

  • Cross-linking experiments, however, illustrate a tight association of HA95 with LBR and LAP2 only [6].
  • We report a role for HA95, a nuclear protein with high homology to the nuclear A-kinase anchoring protein AKAP95, in the regulation of nuclear envelope-chromatin interactions [6].
  • Finally, we showed that HAP95 synergizes significantly with RHA on CTE-mediated reporter gene expression and promotes nuclear export of unspliced mRNA in transfected cells [1].
  • Identification, cloning and characterization of a novel nuclear protein, HA95, homologous to A-kinase anchoring protein 95 [7].


  1. Mapping the functional domains of HAP95, a protein that binds RNA helicase A and activates the constitutive transport element of type D retroviruses. Yang, J.P., Tang, H., Reddy, T.R., Wong-Staal, F. J. Biol. Chem. (2001) [Pubmed]
  2. A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element. Westberg, C., Yang, J.P., Tang, H., Reddy, T.R., Wong-Staal, F. J. Biol. Chem. (2000) [Pubmed]
  3. Protein kinase A associates with HA95 and affects transcriptional coactivation by Epstein-Barr virus nuclear proteins. Han, I., Xue, Y., Harada, S., Orstavik, S., Skalhegg, B., Kieff, E. Mol. Cell. Biol. (2002) [Pubmed]
  4. A novel histone deacetylase pathway regulates mitosis by modulating Aurora B kinase activity. Li, Y., Kao, G.D., Garcia, B.A., Shabanowitz, J., Hunt, D.F., Qin, J., Phelan, C., Lazar, M.A. Genes Dev. (2006) [Pubmed]
  5. HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication. Martins, S., Eikvar, S., Furukawa, K., Collas, P. J. Cell Biol. (2003) [Pubmed]
  6. HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics. Martins, S.B., Eide, T., Steen, R.L., Jahnsen, T., Skålhegg B, S., Collas, P. J. Cell. Sci. (2000) [Pubmed]
  7. Identification, cloning and characterization of a novel nuclear protein, HA95, homologous to A-kinase anchoring protein 95. Orstavik, S., Eide, T., Collas, P., Han, I.O., Taskén, K., Kieff, E., Jahnsen, T., Skålhegg, B.S. Biol. Cell (2000) [Pubmed]
  8. In vitro modulation of the interaction between HA95 and LAP2beta by cAMP signaling. Martins, S.B., Marstad, A., Collas, P. Biochemistry (2003) [Pubmed]
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