The N-terminal RASSF family

a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation

Victoria Sherwood, Asha Recino, Alex Jeffries, Andrew Ward, Andrew D. Chalmers (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    61 Citations (Scopus)

    Abstract

    The RASSF (Ras-association domain family) has recently gained several new members and now contains ten proteins (RASSF1-10), several of which are potential tumour suppressors. The family can be split into two groups, the classical RASSF proteins (RASSF1-6) and the four recently added N-terminal RASSF proteins (RASSF7-10). The N-terminal RASSF proteins have a number of differences from the classical RASSF members and represent a newly defined set of potential Ras effectors. They have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia. Two members of the N-terminal RASSF family have also been highlighted as potential tumour suppressors. The present review will summarize what is known about the N-terminal RASSF proteins, addressing their function and possible links to cancer formation. It will also compare the N-terminal RASSF proteins with the classical RASSF proteins and ask whether the N-terminal RASSF proteins should be considered as genuine members or imposters in the RASSF family.

    Original languageEnglish
    Pages (from-to)303-311
    Number of pages9
    JournalBiochemical Journal
    Volume425
    Issue number2
    DOIs
    Publication statusPublished - 15 Jan 2010

    Fingerprint

    Association reactions
    Neoplasms
    Proteins
    Tumors
    Protein Domains
    Methylation
    Cell death
    Biological Phenomena
    Microtubules
    Cell Death
    Cell Proliferation

    Keywords

    • Cell physiological phenomena
    • Humans
    • Neoplasms
    • Protein structure, Tertiary
    • Transcription factors
    • Tumor suppressor proteins
    • Vesicular transport proteins

    Cite this

    Sherwood, Victoria ; Recino, Asha ; Jeffries, Alex ; Ward, Andrew ; Chalmers, Andrew D. / The N-terminal RASSF family : a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation. In: Biochemical Journal. 2010 ; Vol. 425, No. 2. pp. 303-311.
    @article{3878ef4339cc4d9e8115d0f4f7c4e971,
    title = "The N-terminal RASSF family: a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation",
    abstract = "The RASSF (Ras-association domain family) has recently gained several new members and now contains ten proteins (RASSF1-10), several of which are potential tumour suppressors. The family can be split into two groups, the classical RASSF proteins (RASSF1-6) and the four recently added N-terminal RASSF proteins (RASSF7-10). The N-terminal RASSF proteins have a number of differences from the classical RASSF members and represent a newly defined set of potential Ras effectors. They have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia. Two members of the N-terminal RASSF family have also been highlighted as potential tumour suppressors. The present review will summarize what is known about the N-terminal RASSF proteins, addressing their function and possible links to cancer formation. It will also compare the N-terminal RASSF proteins with the classical RASSF proteins and ask whether the N-terminal RASSF proteins should be considered as genuine members or imposters in the RASSF family.",
    keywords = "Cell physiological phenomena, Humans, Neoplasms, Protein structure, Tertiary, Transcription factors, Tumor suppressor proteins, Vesicular transport proteins",
    author = "Victoria Sherwood and Asha Recino and Alex Jeffries and Andrew Ward and Chalmers, {Andrew D.}",
    year = "2010",
    month = "1",
    day = "15",
    doi = "10.1042/BJ20091318",
    language = "English",
    volume = "425",
    pages = "303--311",
    journal = "Biochemical Journal",
    issn = "0264-6021",
    publisher = "Portland Press",
    number = "2",

    }

    The N-terminal RASSF family : a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation. / Sherwood, Victoria; Recino, Asha; Jeffries, Alex; Ward, Andrew; Chalmers, Andrew D. (Lead / Corresponding author).

    In: Biochemical Journal, Vol. 425, No. 2, 15.01.2010, p. 303-311.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - The N-terminal RASSF family

    T2 - a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation

    AU - Sherwood, Victoria

    AU - Recino, Asha

    AU - Jeffries, Alex

    AU - Ward, Andrew

    AU - Chalmers, Andrew D.

    PY - 2010/1/15

    Y1 - 2010/1/15

    N2 - The RASSF (Ras-association domain family) has recently gained several new members and now contains ten proteins (RASSF1-10), several of which are potential tumour suppressors. The family can be split into two groups, the classical RASSF proteins (RASSF1-6) and the four recently added N-terminal RASSF proteins (RASSF7-10). The N-terminal RASSF proteins have a number of differences from the classical RASSF members and represent a newly defined set of potential Ras effectors. They have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia. Two members of the N-terminal RASSF family have also been highlighted as potential tumour suppressors. The present review will summarize what is known about the N-terminal RASSF proteins, addressing their function and possible links to cancer formation. It will also compare the N-terminal RASSF proteins with the classical RASSF proteins and ask whether the N-terminal RASSF proteins should be considered as genuine members or imposters in the RASSF family.

    AB - The RASSF (Ras-association domain family) has recently gained several new members and now contains ten proteins (RASSF1-10), several of which are potential tumour suppressors. The family can be split into two groups, the classical RASSF proteins (RASSF1-6) and the four recently added N-terminal RASSF proteins (RASSF7-10). The N-terminal RASSF proteins have a number of differences from the classical RASSF members and represent a newly defined set of potential Ras effectors. They have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia. Two members of the N-terminal RASSF family have also been highlighted as potential tumour suppressors. The present review will summarize what is known about the N-terminal RASSF proteins, addressing their function and possible links to cancer formation. It will also compare the N-terminal RASSF proteins with the classical RASSF proteins and ask whether the N-terminal RASSF proteins should be considered as genuine members or imposters in the RASSF family.

    KW - Cell physiological phenomena

    KW - Humans

    KW - Neoplasms

    KW - Protein structure, Tertiary

    KW - Transcription factors

    KW - Tumor suppressor proteins

    KW - Vesicular transport proteins

    U2 - 10.1042/BJ20091318

    DO - 10.1042/BJ20091318

    M3 - Article

    VL - 425

    SP - 303

    EP - 311

    JO - Biochemical Journal

    JF - Biochemical Journal

    SN - 0264-6021

    IS - 2

    ER -