Expression of Unusually Large Keratins During Terminal Differentiation: Balance of Type I and Type II Keratins is Not Disrupted

Overview

Journal J Cell Biol

Specialty Cell Biology

Date 1984 Nov 1

PMID 6208205

Citations 7

Authors

K H Kim

D Marchuk

E Fuchs

Affiliations

Soon will be listed here.

Abstract

When a basal epidermal cell undergoes a commitment to terminally differentiate, it ceases to divide and begins to migrate outward towards the surface of the skin. Dramatic changes in its cytoskeletal architecture take place, accompanied by numerous changes in the expression of keratins, a family of related polypeptides that form 8-nm filaments in these cells. We show here that a shift to the synthesis of unusually large keratins occurs that does not seem to disrupt the ratio of two distinct subfamilies of keratins. Preliminary studies indicate that this differentiation-specific shift may be at the level of transcriptional rather than post-transcriptional regulation. The striking similarities between these large keratins and the type I and type II keratins of basal epidermal cells suggests the important role that both classes of large keratin sequences must play in the assembly of the intermediate filaments within the differentiating keratinocyte.

Citing Articles

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Cohen E, Johnson C, Redmond C, Nair R, Coulombe P J Cell Sci. 2022; 135(20).

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In Vitro Model of the Epidermis: Connecting Protein Function to 3D Structure.

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Structure of a gene for the human epidermal 67-kDa keratin.

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Sequence and expression of a type II keratin, K5, in human epidermal cells.

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Keratin filament composition of human epidermal spinous and granular cell fractions selected by flow cytometric sorting.

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