TY - JOUR
T1 - Subcellular localization and trafficking of phytolongins (non-SNARE longins) in the plant secretory pathway
AU - De Marcos Lousa, Carine
AU - Soubeyrand, Eric
AU - Bolognese, Paolo
AU - Wattelet-Boyer, Valerie
AU - Bouyssou, Guillaume
AU - Marais, Claireline
AU - Boutte, Yohann
AU - Filippini, Francesco
AU - Moreau, Patrick
N1 - Copyright:
© The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology.
PY - 2016/4
Y1 - 2016/4
N2 - SNARE proteins are central elements of the machinery involved in membrane fusion of eukaryotic cells. In animals and plants, SNAREs have diversified to sustain a variety of specific functions. In animals, R-SNARE proteins called brevins have diversified; in contrast, in plants, the R-SNARE proteins named longins have diversified. Recently, a new subfamily of four longins named 'phytolongins' (Phyl) was discovered. One intriguing aspect of Phyl proteins is the lack of the typical SNARE motif, which is replaced by another domain termed the 'Phyl domain'. Phytolongins have a rather ubiquitous tissue expression in Arabidopsis but still await intracellular characterization. In this study, we found that the four phytolongins are distributed along the secretory pathway. While Phyl2.1 and Phyl2.2 are strictly located at the endoplasmic reticulum network, Phyl1.2 associates with the Golgi bodies, and Phyl1.1 locates mainly at the plasma membrane and partially in the Golgi bodies and post-Golgi compartments. Our results show that export of Phyl1.1 from the endoplasmic reticulum depends on the GTPase Sar1, the Sar1 guanine nucleotide exchange factor Sec12, and the SNAREs Sec22 and Memb11. In addition, we have identified the Y48F49 motif as being critical for the exit of Phyl1.1 from the endoplasmic reticulum. Our results provide the first characterization of the subcellular localization of the phytolongins, and we discuss their potential role in regulating the secretory pathway.
AB - SNARE proteins are central elements of the machinery involved in membrane fusion of eukaryotic cells. In animals and plants, SNAREs have diversified to sustain a variety of specific functions. In animals, R-SNARE proteins called brevins have diversified; in contrast, in plants, the R-SNARE proteins named longins have diversified. Recently, a new subfamily of four longins named 'phytolongins' (Phyl) was discovered. One intriguing aspect of Phyl proteins is the lack of the typical SNARE motif, which is replaced by another domain termed the 'Phyl domain'. Phytolongins have a rather ubiquitous tissue expression in Arabidopsis but still await intracellular characterization. In this study, we found that the four phytolongins are distributed along the secretory pathway. While Phyl2.1 and Phyl2.2 are strictly located at the endoplasmic reticulum network, Phyl1.2 associates with the Golgi bodies, and Phyl1.1 locates mainly at the plasma membrane and partially in the Golgi bodies and post-Golgi compartments. Our results show that export of Phyl1.1 from the endoplasmic reticulum depends on the GTPase Sar1, the Sar1 guanine nucleotide exchange factor Sec12, and the SNAREs Sec22 and Memb11. In addition, we have identified the Y48F49 motif as being critical for the exit of Phyl1.1 from the endoplasmic reticulum. Our results provide the first characterization of the subcellular localization of the phytolongins, and we discuss their potential role in regulating the secretory pathway.
KW - ER export YF motif
KW - longin domain
KW - phytolongins
KW - protein targeting
KW - secretory pathway
KW - subcellular localization
UR - http://www.scopus.com/inward/record.url?scp=84969916299&partnerID=8YFLogxK
U2 - 10.1093/jxb/erw094
DO - 10.1093/jxb/erw094
M3 - Article
AN - SCOPUS:84969916299
SN - 0022-0957
VL - 67
SP - 2627
EP - 2639
JO - Journal of Experimental Botany
JF - Journal of Experimental Botany
IS - 9
ER -