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CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain.

Mori, Hidetoshi, Tomari, Taizo, Koshikawa, Naohiko, Kajita, Masahiro, Itoh, Yoshifumi, Sato, Hiroshi, Tojo, Hideaki, Yana, Ikuo, Seiki, Motoharu·2002·The EMBO Journal
DOI 10.1093/emboj/cdf411
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Crossref · 10.1093/emboj/cdf411

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  • Exosites outside the catalytic core domain of MMPs are less conserved and contribute to substrate selection and binding.

    “exosites that are regions outside the catalytic core domain of MMPs are less conserved and contribute to substrate selection and binding (27–29).”

    From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [29]

    The section “The PEX domain of MT1-MMP binds directly to the stem region of CD44H” (page unavailable) shows that a domain outside the catalytic core binds CD44H; the discussion also says that domain is indispensable for CD44H shedding. Our copy does not establish that exosites are less conserved or that they generally govern substrate selection across MMPs. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 48

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Metadata

Authors
Mori, H., Tomari, T., Koshikawa, N., Kajita, M., Itoh, Y., Sato, H., Tojo, H., Yana, I., & Seiki, M.
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2002-08-01
Volume
21
Issue
15
Pages
3949-3959
ISSN
  • 0261-4189
  • 1460-2075
DOI
10.1093/emboj/cdf411
Cited by
296
References
2
Language
en
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