Cited by 1,095Neurofibromatosis and Schwannoma CasesProtein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase Signaling

The neurofibromatosis type 1 gene encodes a protein related to GAP

Xu, Gangfeng, O'Connell, Peter, Viskochil, David, Cawthon, Richard, Robertson, Margaret, Culver, Melanie, Dunn, Diane, Stevens, Jeff +3 more·1990·Cell

Abstract

cDNA walking and sequencing have extended the open reading frame for the neurofibromatosis type 1 gene (NF1). The new sequence now predicts 2485 amino acids of the NF1 peptide. A 360 residue region of the new peptide shows significant similarity to the known catalytic domains of both human and bovine GAP (GTPase activating protein). A much broader region, centered around this same 360 amino acid sequence, is strikingly similar to the yeast IRA1 product, which has a similar amino acid sequence and functional homology to mammalian GAP. This evidence suggests that NF1 encodes a cytoplasmic GAP-like protein that may be involved in the control of cell growth by interacting with proteins such as the RAS gene product. Mapping of the cDNA clones has confirmed that NF1 spans a t(1;17) translocation mutation and that three active genes lie within an intron of NF1, but in opposite orientation.

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Crossref · 10.1016/0092-8674(90)90024-9

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42 of 42 references verified0 citation errors · 0 not checkable

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  • KRAS proteins primarily bind GDP and are in an inactive conformation maintained by intrinsic GTP hydrolytic activity.

    “KRAS proteins primarily bind to guanosine diphosphate (GDP) and are in an inactive conformation maintained by intrinsic guanosine triphosphate (GTP) hydrolytic activity.”

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Authors
Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., & Weiss, R.
Affiliations
  • Howard Hughes Medical Institute (US)
  • University of Utah (US)
Venue
Cell
Publisher
Elsevier BV
Published
1990-08
Volume
62
Issue
3
Pages
599-608
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2159096148
Cited by
1,095
References
42
Citations by year
2026: 7 · 2025: 13 · 2024: 19 · 2023: 19 · 2022: 22 · 2021: 22 · 2020: 22 · 2019: 18 · 2018: 22 · 2017: 17 · 2016: 19 · 2015: 21 · 2014: 24 · 2013: 24 · 2012: 45
FWCI
70.71
Type
journal article
Language
en
Open access
closed
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Howard Hughes Medical Institute
  • U.S. Department of Energy
Topics
  • Health Sciences › Medicine › Neurology › Neurofibromatosis and Schwannoma Cases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
neurofibromatosis type 1, NF1 gene, GTPase-activating protein, Ras, open reading frames, cDNA cloning, cell growth regulation, protein homology
MeSH terms
Amino Acid Sequence, Animals, Base Sequence, Cattle, Chromosomes, Human, Pair 1, Chromosomes, Human, Pair 17, Cloning, Molecular, Genes, Humans, Information Systems, Molecular Sequence Data, Neurofibromatosis 1, Proteins, Sequence Homology, Nucleic Acid, Translocation, Genetic, Oligonucleotide Probes, Gene Library, Polymerase Chain Reaction, GTPase-Activating Proteins, ras GTPase-Activating Proteins, Neurofibromin 1

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