Độ phức tạp phân tử và động học của sự gắn kết giữa tế bào và ma trận

Journal of Cell Science - Tập 114 Số 20 - Trang 3583-3590 - 2001
Eli Zamir1, Benjamin Geiger1
1Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel

Tóm tắt

Hiện nay, hơn 50 protein đã được báo cáo liên quan đến các điểm tiếp xúc khu trú và sự bám dính ECM liên quan. Hầu hết các protein này chứa nhiều miền cho phép chúng tương tác với các đối tác phân tử khác nhau, có khả năng tạo thành một mạng lưới protein dày đặc và không đồng nhất tại các mặt tế bào của điểm bám dính. Đa dạng phân tử và cấu trúc của ‘tấm nhãn phụ’ này được điều chỉnh bởi nhiều cơ chế khác nhau, bao gồm sự cạnh tranh giữa các protein đối tác khác nhau cho các vị trí liên kết giống nhau, các tương tác được kích hoạt hoặc ức chế bởi sự phosphoryl hóa tyrosine, và sự thay đổi hình dạng trong các protein thành phần, có thể ảnh hưởng đến tính phản ứng của chúng. Thực sự, sự bám dính trung gian integrin có thể trải qua những thay đổi động về cấu trúc và tính chất phân tử từ các phức hợp khu trú dạng chấm đến các điểm tiếp xúc khu trú liên kết với sợi căng thẳng, có thể ‘chín muồi’ hơn để hình thành sự bám dính dạng sợi liên kết với fibronectin. Những thay đổi này được thúc đẩy bởi lực cơ học do máy móc co bóp chứa actin và myosin của tế bào tạo ra, hoặc bởi các lực bên ngoài tác động lên tế bào, và được điều chỉnh bởi độ cứng của ma trận.

Từ khóa


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