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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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RHPN2  -  rhophilin, Rho GTPase binding protein 2

Homo sapiens

Synonyms: 76 kDa RhoB effector protein, GTP-Rho-binding protein 2, P76RBE, RHOBP, Rhophilin-2, ...
 
 
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High impact information on RHPN2

  • The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization [1].
  • Based on the biochemical and biological activity, Rhophilin-2 may function normally in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity [1].
  • Although Rhophilin-2-expressing HeLa cells showed a loss of actin stress fibers, Rhophilin-1 expression had no noticeable effect on the actin cytoskeleton [1].
  • Rhophilin-2 or p76(RBE), a protein whose expression is induced by the cyclic AMP pathway in thyrocytes, contains several protein-protein interaction domains including HR-1, Bro1 and PDZ domains, and is a partner of RhoB in its GTP-bound form (Eur J Biochem, 269(24): 6241-9, 2002) [2].
  • By subcellular fractionation and colocalization experiments, rhophilin-2 is recruited to subcellular organelles by activated RhoB-GTP [2].
 

Biological context of RHPN2

  • Our data suggest that p76RBE could play a key role between RhoB and potential downstream elements needed under stimulation of the thyrotropin/cAMP pathway in thyrocytes and responsible for intracellular motile phenomena such as the endocytosis involved in the thyroid secretory process [3].

References

  1. The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization. Peck, J.W., Oberst, M., Bouker, K.B., Bowden, E., Burbelo, P.D. J. Biol. Chem. (2002) [Pubmed]
  2. Rhophilin-2 is targeted to late-endosomal structures of the vesicular machinery in the presence of activated RhoB. Steuve, S., Devosse, T., Lauwers, E., Vanderwinden, J.M., Andr??, B., Courtoy, P.J., Pirson, I. Exp. Cell Res. (2006) [Pubmed]
  3. Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP. Mircescu, H., Steuve, S., Savonet, V., Degraef, C., Mellor, H., Dumont, J.E., Maenhaut, C., Pirson, I. Eur. J. Biochem. (2002) [Pubmed]
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