Spatiotemporal organization, regulation and function of traction during neutrophil chemotaxis

Shin, Myung Eun

Permalink

https://hdl.handle.net/2142/29509 Copy

Description

Title

Spatiotemporal organization, regulation and function of traction during neutrophil chemotaxis

Author(s)

Shin, Myung Eun

Issue Date

2012-02-01T00:49:57Z

Director of Research (if dissertation) or Advisor (if thesis)

Wang, Fei

Doctoral Committee Chair(s)

Belmont, Andrew S.

Committee Member(s)

• Wang, Fei
• Chen, Jie
• Newmark, Phillip A.
• Xiang, Yang

Department of Study

Cell & Developmental Biology

Discipline

Cell and Developmental Biology

Degree Granting Institution

University of Illinois at Urbana-Champaign

Degree Name

Ph.D.

Degree Level

Dissertation

Keyword(s)

• Neutrophil Chemotaxis
• Traction
• Myosin-Light-Chain Kinase
• Myosin Type II
• Cell Adhesion
• Cell Motility
• Mechanotransduction

Abstract

Despite recent advances in our understanding of biochemical regulation of neutrophil chemotaxis, little is known about how mechanical factors control neutrophils’ persistent polarity and rapid motility. Here, by using a human neutrophil-like cell line and human primary neutrophils, we describe a dynamic spatiotemporal pattern of tractions in neutrophils during chemotaxis. Tractions are located at both the leading and the trailing edge of neutrophils, where they oscillate with a defined periodicity. Interestingly, traction oscillations at the leading and the trailing edge are out of phase with the tractions at the front leading those at the back, suggesting a temporal mechanism that coordinates leading edge and trailing edge activities. The magnitude and periodicity of tractions depend upon the activity of non-muscle myosin IIA. Specifically, traction development at the leading edge requires myosin light chain kinase (MLCK)-mediated myosin II contractility and is necessary for α5β1-integrin activation and leading edge adhesion. Localized myosin II activation induced by spatially activated small GTPase Rho and its downstream kinase p160-ROCK, as previously reported, leads to contraction of actin-myosin II complexes at the trailing edge, causing it to de-adhere. Our data identify a key biomechanical mechanism for persistent cell polarity and motility.

Graduation Semester

2011-12

Permalink

http://hdl.handle.net/2142/29509

Copyright and License Information

Copyright 2011 Myung Eun Shin

Owning Collections