| Description | The Ras association domain (RASSF) proteins are named due to the presence of a Ras association (RA) domain in their N or C terminus that can potentially interact with the Ras GTPase family of proteins. These GTPases control a variety of cellular processes, such as membrane trafficking, apoptosis, and proliferation. RASSF proteins contain several other functional domains that modulate associations with other proteins. RASSF proteins with the RA domain at the C terminus (which are termed C-terminal or classical RASSF) usually also include a Salvador-RASSF-Hippo (SARAH) domain involved in several protein-protein interactions and for homo- and heterodimerisation of RASSF isoforms. N-terminal RASSF proteins (with the RA domain in the N terminus) do not usually contain a SARAH domain [ ].At least 10 RASSF family members have been characterised (with multiple splice variants), many of which have been shown to play a role in tumour suppression. RASSF proteins also act as scaffolding agents in microtubule stability, regulate mitotic cell division, control cell migration and cell adhesion, and modulate NF-KB activity and the duration of inflammation. Loss of RASSF expression through promoter methylation has been shown in numerous types of cancer, including leukemia, melanoma, breast and prostate cancer [ ].RASSF1 is one of the C-terminal (also known as classical) RASSF proteins, characterised by an RA domain and a SARAH domain ( ) in the C terminus [ ]. Human RASSF1 has multiple transcripts as a result of alternative splicing and differential promoter usage. RASSF1A and 1C are the most widely studied and characterised of these. While they are both involved in regulation of growth and migration via microtubule localization, they have very different biological properties [].RASSF1A is a tumour suppressor primarily important in microtubule stability, but implicated in a number of different functions, including cell-cycle regulation, spindle assembly, chromosome attachment, apoptosis and inflammation control, amongst others [ ].In contrast, RASSF1C has not been shown to be a tumour suppressor, and has even been implicated as an oncogene by a number of mechanisms [ ]. It has been reported to activate cell proliferation through interaction with IGFBP-5, and may also interact with TFPI-2, which is involved in angiogenesis and tumour growth/metastasis [, ]. RASSF1C has also been reported to interact with and stabilise microtubules [].This entry represents the Ras-associating (RA) domain of RASSF1, which has a β-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases. | Name | Ras association domain-containing protein 1, RA domain |
| Short Name | RASSF1_RA | Type | Domain |
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