![]() Garcia-Dominguez M, Reyes JC (2009) SUMO association with repressor complexes, emerging routes for transcriptional control. Matic I, Schimmel J, Hendriks IA et al (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Zhang X-D, Goeres J, Zhang H et al (2008) SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Matunis MJ, Coutavas E, Blobel G (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. Cell 88:97–107īossis G, Malnou CE, Farras R et al (2005) Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation. Mahajan R, Delphin C, Guan T et al (1997) A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Soderberg O, Gullberg M, Jarvius M et al (2006) Direct observation of individual endogenous protein complexes in situ by proximity ligation. Tempé D, Vives E, Brockly F et al (2014) SUMOylation of the inducible (c-Fos:c-Jun)/AP-1 transcription complex occurs on target promoters to limit transcriptional activation. Hay RT (2005) SUMO: a history of modification. Key wordsįlotho A, Melchior F (2013) Sumoylation: a regulatory protein modification in health and disease. Here, we describe the use of PLA to detect protein SUMOylation, a posttranslational modification related to ubiquitination, as well as interaction of SUMOylated substrates with other proteins, using both adherent and suspension cells. Another application of this technique is the detection of proteins posttranslational modifications to monitor their localization and dynamics in situ. PLA relies on the use of combinations of antibodies coupled to complementary oligonucleotides that are amplified and revealed with a fluorescent probe, each spot representing a single protein–protein interaction. The recent development of the proximity ligation assays (PLA) technology allows easy visualization of endogenous protein–protein interactions at the single molecule level. ![]() The detection of protein–protein interactions by imaging techniques often requires the overexpression of the proteins of interest tagged with fluorescent molecules, which can affect their biological properties and, subsequently, flaw experiment interpretations. ![]()
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