Abstract
The vav proto-oncogene is exclusively expressed in hematopoietic cells and encodes a 95-kDa protein that contains multiple structural domains. Vav is involved in the expansion of T and B cells, in antigen-mediated proliferative responses, and in the induction of intrathymic T cell maturation. It becomes rapidly and transiently tyrosine-phosphorylated upon triggering of a large number of surface receptors and catalyzes GDP/GTP exchange on Rac-1. We now provide evidence for the specific interaction of Vav with heterogeneous nuclear ribonucleoprotein (hnRNP) C. Vav and hnRNP C interact both in vive and in vitro mediated through the carboxyl Src homology 3 domain of Vav and the proline-rich motif located in the nuclear retention sequence of hnRNP C. More importantly, Vav-hnRNP C complexes are present in living hematopoietic cells and both proteins localize in the nuclei, mainly on perichromatic fibrils but also on clusters of interchromatin granules. The Vav-hnRNP C interaction is regulated by poly(U) RNA, although a basal association is still detected in the absence of RNA. Furthermore, RNA homopolymers differentially alter the binding affinity of Vav to hnRNP C and hnRNP K. We propose that Vav-hnRNP interactions may be established in an RNA- dependent manner.
| Original language | English |
|---|---|
| Pages (from-to) | 5923-5931 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 273 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Mar 6 1998 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C : Evidence for Vav-hnRNP interactions in an RNA-dependent manner. / Romero, Francisco; Germani, Antonia; Puvion, Edmond; Camonis, Jacques; Varin-Blank, Nadine; Gisselbrecht, Sylvie; Fischer, Siegmund.
In: Journal of Biological Chemistry, Vol. 273, No. 10, 06.03.1998, p. 5923-5931.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C
T2 - Evidence for Vav-hnRNP interactions in an RNA-dependent manner
AU - Romero, Francisco
AU - Germani, Antonia
AU - Puvion, Edmond
AU - Camonis, Jacques
AU - Varin-Blank, Nadine
AU - Gisselbrecht, Sylvie
AU - Fischer, Siegmund
PY - 1998/3/6
Y1 - 1998/3/6
N2 - The vav proto-oncogene is exclusively expressed in hematopoietic cells and encodes a 95-kDa protein that contains multiple structural domains. Vav is involved in the expansion of T and B cells, in antigen-mediated proliferative responses, and in the induction of intrathymic T cell maturation. It becomes rapidly and transiently tyrosine-phosphorylated upon triggering of a large number of surface receptors and catalyzes GDP/GTP exchange on Rac-1. We now provide evidence for the specific interaction of Vav with heterogeneous nuclear ribonucleoprotein (hnRNP) C. Vav and hnRNP C interact both in vive and in vitro mediated through the carboxyl Src homology 3 domain of Vav and the proline-rich motif located in the nuclear retention sequence of hnRNP C. More importantly, Vav-hnRNP C complexes are present in living hematopoietic cells and both proteins localize in the nuclei, mainly on perichromatic fibrils but also on clusters of interchromatin granules. The Vav-hnRNP C interaction is regulated by poly(U) RNA, although a basal association is still detected in the absence of RNA. Furthermore, RNA homopolymers differentially alter the binding affinity of Vav to hnRNP C and hnRNP K. We propose that Vav-hnRNP interactions may be established in an RNA- dependent manner.
AB - The vav proto-oncogene is exclusively expressed in hematopoietic cells and encodes a 95-kDa protein that contains multiple structural domains. Vav is involved in the expansion of T and B cells, in antigen-mediated proliferative responses, and in the induction of intrathymic T cell maturation. It becomes rapidly and transiently tyrosine-phosphorylated upon triggering of a large number of surface receptors and catalyzes GDP/GTP exchange on Rac-1. We now provide evidence for the specific interaction of Vav with heterogeneous nuclear ribonucleoprotein (hnRNP) C. Vav and hnRNP C interact both in vive and in vitro mediated through the carboxyl Src homology 3 domain of Vav and the proline-rich motif located in the nuclear retention sequence of hnRNP C. More importantly, Vav-hnRNP C complexes are present in living hematopoietic cells and both proteins localize in the nuclei, mainly on perichromatic fibrils but also on clusters of interchromatin granules. The Vav-hnRNP C interaction is regulated by poly(U) RNA, although a basal association is still detected in the absence of RNA. Furthermore, RNA homopolymers differentially alter the binding affinity of Vav to hnRNP C and hnRNP K. We propose that Vav-hnRNP interactions may be established in an RNA- dependent manner.
UR - http://www.scopus.com/inward/record.url?scp=0032489365&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032489365&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.10.5923
DO - 10.1074/jbc.273.10.5923
M3 - Article
C2 - 9488731
AN - SCOPUS:0032489365
VL - 273
SP - 5923
EP - 5931
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 10
ER -