Self-organization of keratin intermediate filaments into cross-linked networks

Chang Hun Lee, Pierre A. Coulombe

Research output: Contribution to journalArticle

Abstract

Keratins, the largest subgroup of intermediate filament (IF) proteins, form a network of 10-nm filaments built from type I/II heterodimers in epithelial cells. A major function of keratin IFs is to protect epithelial cells from mechanical stress. Like filamentous actin, keratin IFs must be cross-linked in vitro to achieve the high level of mechanical resilience characteristic of live cells. Keratins 5 and 14 (K5 and K14), the main pairing occurring in the basal progenitor layer of epidermis and related epithelia, can readily self-organize into large filament bundles in vitro and in vivo. Here, we show that filament self-organization is mediated by multivalent interactions involving distinct regions in K5 and K14 proteins. Selforganization is determined independently of polymerization into 10-nm filaments, but involves specific type I-type II keratin complementarity. We propose that self-organization is a key determinant of the structural support function of keratin IFs in vivo.

Original languageEnglish (US)
Pages (from-to)409-421
Number of pages13
JournalJournal of Cell Biology
Volume186
Issue number3
DOIs
StatePublished - Aug 10 2009

Fingerprint

Intermediate Filaments
Keratins
Type I Keratin
Type II Keratin
Epithelial Cells
Keratin-14
Keratin-5
Intermediate Filament Proteins
Mechanical Stress
Epidermis
Polymerization
Actins
Epithelium
Proteins
In Vitro Techniques

ASJC Scopus subject areas

  • Cell Biology

Cite this

Self-organization of keratin intermediate filaments into cross-linked networks. / Lee, Chang Hun; Coulombe, Pierre A.

In: Journal of Cell Biology, Vol. 186, No. 3, 10.08.2009, p. 409-421.

Research output: Contribution to journalArticle

Lee, Chang Hun ; Coulombe, Pierre A. / Self-organization of keratin intermediate filaments into cross-linked networks. In: Journal of Cell Biology. 2009 ; Vol. 186, No. 3. pp. 409-421.
@article{8e6f99cea1ab43ce9b92661c5db63f9e,
title = "Self-organization of keratin intermediate filaments into cross-linked networks",
abstract = "Keratins, the largest subgroup of intermediate filament (IF) proteins, form a network of 10-nm filaments built from type I/II heterodimers in epithelial cells. A major function of keratin IFs is to protect epithelial cells from mechanical stress. Like filamentous actin, keratin IFs must be cross-linked in vitro to achieve the high level of mechanical resilience characteristic of live cells. Keratins 5 and 14 (K5 and K14), the main pairing occurring in the basal progenitor layer of epidermis and related epithelia, can readily self-organize into large filament bundles in vitro and in vivo. Here, we show that filament self-organization is mediated by multivalent interactions involving distinct regions in K5 and K14 proteins. Selforganization is determined independently of polymerization into 10-nm filaments, but involves specific type I-type II keratin complementarity. We propose that self-organization is a key determinant of the structural support function of keratin IFs in vivo.",
author = "Lee, {Chang Hun} and Coulombe, {Pierre A.}",
year = "2009",
month = "8",
day = "10",
doi = "10.1083/jcb.200810196",
language = "English (US)",
volume = "186",
pages = "409--421",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "3",

}

TY - JOUR

T1 - Self-organization of keratin intermediate filaments into cross-linked networks

AU - Lee, Chang Hun

AU - Coulombe, Pierre A.

PY - 2009/8/10

Y1 - 2009/8/10

N2 - Keratins, the largest subgroup of intermediate filament (IF) proteins, form a network of 10-nm filaments built from type I/II heterodimers in epithelial cells. A major function of keratin IFs is to protect epithelial cells from mechanical stress. Like filamentous actin, keratin IFs must be cross-linked in vitro to achieve the high level of mechanical resilience characteristic of live cells. Keratins 5 and 14 (K5 and K14), the main pairing occurring in the basal progenitor layer of epidermis and related epithelia, can readily self-organize into large filament bundles in vitro and in vivo. Here, we show that filament self-organization is mediated by multivalent interactions involving distinct regions in K5 and K14 proteins. Selforganization is determined independently of polymerization into 10-nm filaments, but involves specific type I-type II keratin complementarity. We propose that self-organization is a key determinant of the structural support function of keratin IFs in vivo.

AB - Keratins, the largest subgroup of intermediate filament (IF) proteins, form a network of 10-nm filaments built from type I/II heterodimers in epithelial cells. A major function of keratin IFs is to protect epithelial cells from mechanical stress. Like filamentous actin, keratin IFs must be cross-linked in vitro to achieve the high level of mechanical resilience characteristic of live cells. Keratins 5 and 14 (K5 and K14), the main pairing occurring in the basal progenitor layer of epidermis and related epithelia, can readily self-organize into large filament bundles in vitro and in vivo. Here, we show that filament self-organization is mediated by multivalent interactions involving distinct regions in K5 and K14 proteins. Selforganization is determined independently of polymerization into 10-nm filaments, but involves specific type I-type II keratin complementarity. We propose that self-organization is a key determinant of the structural support function of keratin IFs in vivo.

UR - http://www.scopus.com/inward/record.url?scp=68549090936&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=68549090936&partnerID=8YFLogxK

U2 - 10.1083/jcb.200810196

DO - 10.1083/jcb.200810196

M3 - Article

VL - 186

SP - 409

EP - 421

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 3

ER -