Tankyrase-1 assembly to large protein complexes blocks its telomeric function
نویسندگان
چکیده
منابع مشابه
Association states of nucleosome assembly protein 1 and its complexes with histones.
The histone chaperone NAP1 is a carrier of histones during nuclear import, nucleosome assembly, and chromatin remodeling. Analytical ultracentrifugation was used to determine the association states of NAP1 alone and in complexes with core histones. In addition, the concentration dependence of the association was quantified by determining the equilibrium dissociation constant between different N...
متن کاملTankyrase 1 regulates centrosome function by controlling CPAP stability.
CPAP--a gene mutated in primary microcephaly--is required for procentriole formation. Here we show that CPAP degradation and function is controlled by the poly(ADP-ribose) polymerase tankyrase 1. CPAP is PARsylated by tankyrase 1 in vitro and in vivo. Overexpression of tankyrase 1 leads to CPAP proteasomal degradation, preventing centriole duplication, whereas depletion of tankyrase 1 stabilize...
متن کاملTankyrase, a poly(ADP-ribose) polymerase at human telomeres.
Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP), was identified and localized to human telomeres. Tankyrase binds to the telomeric protein TRF1 (telomeric repeat binding factor-1), a negative regulator of telomere length maintenance. Like ankyrins, tankyrase contains 24 ankyrin repeats in a domain responsible for...
متن کاملLateral assembly of the immunoglobulin protein SynCAM 1 controls its adhesive function and instructs synapse formation.
Synapses are specialized adhesion sites between neurons that are connected by protein complexes spanning the synaptic cleft. These trans-synaptic interactions can organize synapse formation, but their macromolecular properties and effects on synaptic morphology remain incompletely understood. Here, we demonstrate that the synaptic cell adhesion molecule SynCAM 1 self-assembles laterally via its...
متن کاملHomomeric protein complexes: evolution and assembly.
Homo-oligomeric protein complexes are functionally vital and highly abundant in living cells. In the present article, we review our current understanding of their geometry and evolution, including aspects of the symmetry of these complexes and their interaction interfaces. Also, we briefly discuss the pathway of their assembly in solution.
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2010
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2010.07.062