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2016 ; 9
(420
): ra31
Nephropedia Template TP
gab.com Text
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English Wikipedia
A large Rab GTPase encoded by CRACR2A is a component of subsynaptic vesicles that
transmit T cell activation signals
#MMPMID27016526
Srikanth S
; Kim KD
; Gao Y
; Woo JS
; Ghosh S
; Calmettes G
; Paz A
; Abramson J
; Jiang M
; Gwack Y
Sci Signal
2016[Mar]; 9
(420
): ra31
PMID27016526
show ga
More than 60 members of the Rab family of guanosine triphosphatases (GTPases)
exist in the human genome. Rab GTPases are small proteins that are primarily
involved in the formation, trafficking, and fusion of vesicles. We showed
thatCRACR2A(Ca(2+) release-activated Ca(2+) channel regulator 2A) encodes a
lymphocyte-specific large Rab GTPase that contains multiple functional domains,
including EF-hand motifs, a proline-rich domain (PRD), and a Rab GTPase domain
with an unconventional prenylation site. Through experiments involving gene
silencing in cells and knockout mice, we demonstrated a role for CRACR2A in the
activation of the Ca(2+) and c-Jun N-terminal kinase signaling pathways in
response to T cell receptor (TCR) stimulation. Vesicles containing this Rab
GTPase translocated from near the Golgi to the immunological synapse formed
between a T cell and a cognate antigen-presenting cell to activate these
signaling pathways. The interaction between the PRD of CRACR2A and the guanidine
nucleotide exchange factor Vav1 was required for the accumulation of these
vesicles at the immunological synapse. Furthermore, we demonstrated that GTP
binding and prenylation of CRACR2A were associated with its localization near the
Golgi and its stability. Our findings reveal a previously uncharacterized
function of a large Rab GTPase and vesicles near the Golgi in TCR signaling.
Other GTPases with similar domain architectures may have similar functions in T
cells.
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