Rab GTPases, which form the largest branch of the Ras GTPase superfamily, regulate almost every step of vesicle-mediated trafficking. Among them, Rab8 is an essential participant in primary cilium formation. In a report recently published in the Journal of Cell Science, Finetti and colleagues identify Rab8 as a novel player in vesicular traffic in the non-ciliated T lymphocytes, which contributes to the assembly of the specialized signaling platform known as the immune synapse. By interacting with the v-SNARE VAMP-3, Rab8 is indeed responsible for the final docking/fusion step in T cell receptor (TCR) recycling to the immune synapse. A second important take-home message which comes to light from this work is that VAMP-3 also interacts with Rab8 at the base of the cilium in NIH-3T3 cells, where it regulates ciliary growth and targeting of Smoothened at the plasma membrane. Hence the data presented in this report, in addition to identifying Rab8 as a novel player in vesicular traffic to the immune synapse, reveal how both ciliated and non-ciliated cells take advantage of a conserved pathway to build highly specific cellular structures.

Patrussi, L., Baldari, C. (2016). The Rab GTPase Rab8 as a shared regulator of ciliogenesis and immune synapse assembly: from a conserved pathway to diverse cellular structures. SMALL GTPASES, 7(1), 16-20 [10.1080/21541248.2015.1111852].

The Rab GTPase Rab8 as a shared regulator of ciliogenesis and immune synapse assembly: from a conserved pathway to diverse cellular structures

Patrussi, Laura;Baldari, Cosima
2016-01-01

Abstract

Rab GTPases, which form the largest branch of the Ras GTPase superfamily, regulate almost every step of vesicle-mediated trafficking. Among them, Rab8 is an essential participant in primary cilium formation. In a report recently published in the Journal of Cell Science, Finetti and colleagues identify Rab8 as a novel player in vesicular traffic in the non-ciliated T lymphocytes, which contributes to the assembly of the specialized signaling platform known as the immune synapse. By interacting with the v-SNARE VAMP-3, Rab8 is indeed responsible for the final docking/fusion step in T cell receptor (TCR) recycling to the immune synapse. A second important take-home message which comes to light from this work is that VAMP-3 also interacts with Rab8 at the base of the cilium in NIH-3T3 cells, where it regulates ciliary growth and targeting of Smoothened at the plasma membrane. Hence the data presented in this report, in addition to identifying Rab8 as a novel player in vesicular traffic to the immune synapse, reveal how both ciliated and non-ciliated cells take advantage of a conserved pathway to build highly specific cellular structures.
2016
Patrussi, L., Baldari, C. (2016). The Rab GTPase Rab8 as a shared regulator of ciliogenesis and immune synapse assembly: from a conserved pathway to diverse cellular structures. SMALL GTPASES, 7(1), 16-20 [10.1080/21541248.2015.1111852].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/982783