A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats

James Way, Mark Hellmich, Howard Jaffe, Ben Szaro, Harish C. Pant, Harold Gainer, James Battey

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Previous studies have shown that two low molecular-weight neurofilament (NF) proteins (NF-60 and NF-70) from the squid Loligo pealei are translated from mRNAs that are splice variants of a single squid NF gene. In this study, we report the isolation and characterization of cDNA clones encoding a high-molecular-weight squid NF protein (NF-220), the mRNA of which derives from the same squid NF gene. All three proteins are identical in their amino-terminal and lamin-like rod domains but differ in their carboxyl-terminal tail regions. In contrast to the short tail domains of NF-60 and NF-70, the NF-220 protein has a longer tail domain containing an acidic cluster of amino acids immediately followed by repeated copies of the sequence motif Lys-Ser-Pro. The Lys-Ser-Pro domain is similar to that of mammalian medium NF (NF-M) and high NF (NF-H) proteins, where the serines are highly phosphorylated. Except for these Lys-Ser-Pro motifs, there is surprisingly little structural similarity between the squid NF-220 protein and mammalian NF-M and NF-H proteins. Furthermore, the location of introns in squid NF-220 protein shows that it is more closely related to nuclear lamins and type III intermediate-filament proteins than to vertebrate NF proteins.

Original languageEnglish (US)
Pages (from-to)6963-6967
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number15
StatePublished - 1992
Externally publishedYes

Fingerprint

Lamins
Decapodiformes
Intermediate Filaments
Tail
Neurofilament Proteins
neurofilament protein H
Loligo
Acidic Amino Acids
Intermediate Filament Proteins
Messenger RNA
Introns
Serine
Genes
Vertebrates
Complementary DNA
Clone Cells

Keywords

  • Alternative splicing
  • Intermediate filament
  • Lamin
  • Phosphorylation

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats. / Way, James; Hellmich, Mark; Jaffe, Howard; Szaro, Ben; Pant, Harish C.; Gainer, Harold; Battey, James.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 15, 1992, p. 6963-6967.

Research output: Contribution to journalArticle

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T1 - A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats

AU - Way, James

AU - Hellmich, Mark

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AU - Pant, Harish C.

AU - Gainer, Harold

AU - Battey, James

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AB - Previous studies have shown that two low molecular-weight neurofilament (NF) proteins (NF-60 and NF-70) from the squid Loligo pealei are translated from mRNAs that are splice variants of a single squid NF gene. In this study, we report the isolation and characterization of cDNA clones encoding a high-molecular-weight squid NF protein (NF-220), the mRNA of which derives from the same squid NF gene. All three proteins are identical in their amino-terminal and lamin-like rod domains but differ in their carboxyl-terminal tail regions. In contrast to the short tail domains of NF-60 and NF-70, the NF-220 protein has a longer tail domain containing an acidic cluster of amino acids immediately followed by repeated copies of the sequence motif Lys-Ser-Pro. The Lys-Ser-Pro domain is similar to that of mammalian medium NF (NF-M) and high NF (NF-H) proteins, where the serines are highly phosphorylated. Except for these Lys-Ser-Pro motifs, there is surprisingly little structural similarity between the squid NF-220 protein and mammalian NF-M and NF-H proteins. Furthermore, the location of introns in squid NF-220 protein shows that it is more closely related to nuclear lamins and type III intermediate-filament proteins than to vertebrate NF proteins.

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