Evidence map›Paper›PMID 24603432›Full record

ArticlePlant signaling & behavior2014

Identification of evolutionarily conserved amino acid residues in homeodomain of KNOX proteins for intercellular trafficking.

Huan Chen, David Jackson, Jae-Yean Kim

Abstract read
In one paragraph

Article in Plant signaling & behavior, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Huan ChenDivision of Applied Life Science (BK21plus); Plant Molecular Biology & Biotechnology Research Center; Gyeongsang National University; Jinju, Korea.
David JacksonCold Spring Harbor Laboratory; Cold Spring Harbor, NY USA.
Jae-Yean KimDivision of Applied Life Science (BK21plus); Plant Molecular Biology & Biotechnology Research Center; Gyeongsang National University; Jinju, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maize knotted (KN1) homeodomain (HD) protein is a well-known mobile transcription factor crucial for stem cell maintenance. Recent studies have revealed that the trihelical HD of knotted1-like homeobox (KNOX) proteins is necessary and sufficient for selective cell-to-cell trafficking. Also, the efficient trafficking ability for HD is likely to be acquired during the evolution of early nonvascular land plants. Here, using the point-mutated HD of KN1 and shoot meristemless (STM) in the trichome rescue system, together with molecular structure modeling, we have found the evolutionarily conserved amino acid residues, such as arginine in helix α1 and leucine in helix α3, which are essential for intercellular trafficking. Our studies provided important clues for the 3-dimensional protein structure required for cell-to-cell movement of non-cell-autonomous transcription factors.

Indexed as

Amino Acid SequenceConserved SequenceHomeodomain ProteinsMolecular Sequence DataPlant ProteinsProtein TransportZea maysHomeodomain ProteinsPlant Proteinshomeodomainintercellular protein traffickingnon-cell-autonomousplasmodesmatatranscription factor

Identifiers

PMID24603432
PMCPMC4091555

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.