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Zientara-Rytter K, Sirko A. Significant role of PB1 and UBA domains in multimerization of Joka2, a selective autophagy cargo receptor from tobacco. Front Plant Sci. 2014;5:13doi: 10.3389/fpls.2014.00013.
Zientara-Rytter, K., & Sirko, A. (2014). Significant role of PB1 and UBA domains in multimerization of Joka2, a selective autophagy cargo receptor from tobacco. Frontiers in plant science, 513. https://doi.org/10.3389/fpls.2014.00013
Zientara-Rytter, Katarzyna, and Sirko, Agnieszka. "Significant role of PB1 and UBA domains in multimerization of Joka2, a selective autophagy cargo receptor from tobacco." Frontiers in plant science vol. 5 (2014): 13. doi: https://doi.org/10.3389/fpls.2014.00013
Zientara-Rytter K, Sirko A. Significant role of PB1 and UBA domains in multimerization of Joka2, a selective autophagy cargo receptor from tobacco. Front Plant Sci. 2014 Jan 31;5:13. doi: 10.3389/fpls.2014.00013. eCollection 2014. PMID: 24550923; PMCID: PMC3907767.
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Front Plant Sci. 2014 Jan 31;5:13. doi: 10.3389/fpls.2014.00013. eCollection 2014.

Significant role of PB1 and UBA domains in multimerization of Joka2, a selective autophagy cargo receptor from tobacco.

Frontiers in plant science

Katarzyna Zientara-Rytter, Agnieszka Sirko

Affiliations

  1. Department of Plant Biochemistry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences Warsaw, Poland.

PMID: 24550923 PMCID: PMC3907767 DOI: 10.3389/fpls.2014.00013

Abstract

Tobacco Joka2 protein is a hybrid homolog of two mammalian selective autophagy cargo receptors, p62 and NBR1. These proteins can directly interact with the members of ATG8 family and the polyubiquitinated cargoes designed for degradation. Function of the selective autophagy cargo receptors relies on their ability to form protein aggregates. It has been shown that the N-terminal PB1 domain of p62 is involved in formation of aggregates, while the UBA domains of p62 and NBR1 have been associated mainly with cargo binding. Here we focus on roles of PB1 and UBA domains in localization and aggregation of Joka2 in plant cells. We show that Joka2 can homodimerize not only through its N-terminal PB1-PB1 interactions but also via interaction between N-terminal PB1 and C-terminal UBA domains. We also demonstrate that Joka2 co-localizes with recombinant ubiquitin and sequestrates it into aggregates and that C-terminal part (containing UBA domains) is sufficient for this effect. Our results indicate that Joka2 accumulates in cytoplasmic aggregates and suggest that in addition to these multimeric forms it also exists in the nucleus and cytoplasm in a monomeric form.

Keywords: Joka2; NBR1; PB1; UBA; autophagy; proteasome; selective autophagy cargo receptor; ubiquitin

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