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Query
Condition	Concatenation	Type	Data Entry	Comparison	Numerics	Sentence Range	Exact Match?	Case Sensitive?	Literatures	Fields
0	&&	keyword	TPKB	>	0	sentence	no	no	oryza	body, title, abstract

6 matches found in 2 documents. Results sorted by score (hits) .


Score: 7.00
Title: Rice two-pore K+ channels are expressed in different types of vacuoles .
Author: Isayenkov S Isner JC Maathuis FJ
Journal: Plant Cell Citation: V : 23 P : 756-68 Year: 2011 Type: MEDLINE
Literature: oryza Field: abstract Doc ID: pub21224427 Accession (PMID): 21224427
Abstract: Potassium ( K+ ) is a major nutrient for plant growth and development . Vacuolar K+ ion channels of the two-pore K+ ( TPK ) family play an important role in maintaining K+ homeostasis . Several TPK channels were previously shown to be expressed in the lytic vacuole ( LV ) tonoplast Plants also contain smaller protein storage vacuoles ( PSVs ) that contain membrane transporters . However , the mechanisms that define how membrane proteins reach different vacuolar destinations are largely unknown . The Oryza sativa genome encodes two TPK isoforms ( TPKa and TPKb ) that have very similar sequences and are ubiquitously expressed . The electrophysiological properties of both TPKs were comparable , showing inward rectification and voltage independence . In spite of high levels of similarity in sequence and transport properties , the cellular localization of TPKa and TPKb channels was different , with TPKa localization predominantly at the large LV and TPKb primarily in smaller PSV-type compartments . Trafficking of TPKa was sensitive to brefeldin A , while that of TPKb was not . The use of TPKa : TPKb chimeras showed that C-terminal domains are crucial for the differential targeting of TPKa and TPKb . Site-directed mutagenesis of C-terminal residues that were different between TPKa and TPKb identified three amino acids that are important in determining ultimate vacuolar destination .
Matching Sentences: [ Sen. 7, subscore: 2.00 ]: In spite of high levels of similarity in sequence and transport properties , the cellular localization of TPKa and TPKb channels was different , with TPKa localization predominantly at the large LV and TPKb primarily in smaller PSV-type compartments . [ Sen. 9, subscore: 2.00 ]: The use of TPKa : TPKb chimeras showed that C-terminal domains are crucial for the differential targeting of TPKa and TPKb . [ Sen. 5, subscore: 1.00 ]: The Oryza sativa genome encodes two TPK isoforms ( TPKa and TPKb ) that have very similar sequences and are ubiquitously expressed . [ Sen. 8, subscore: 1.00 ]: Trafficking of TPKa was sensitive to brefeldin A , while that of TPKb was not . [ Sen. 10, subscore: 1.00 ]: Site-directed mutagenesis of C-terminal residues that were different between TPKa and TPKb identified three amino acids that are important in determining ultimate vacuolar destination .
Supplemental links/files: reference in endnote online text related articles pubmed citation


Score: 1.00
Title: Membrane localisation diversity of TPK channels and their physiological role .
Author: Isayenkov S Isner JC Maathuis FJ
Journal: Plant Signal Behav Citation: V : 6 P : 1201-4 Year: 2011 Type: In-Process
Literature: oryza Field: abstract Doc ID: pub21757998 Accession (PMID): 21757998
Abstract: Potassium ( K ) is one of the major nutrients that is essential for plant growth and development . The majority of cellular K+ resides in the vacuole and tonoplast K+ channels of the TPK ( Two Pore K ) family are main players in cellular K+ homeostasis . All TPK channels were previously reported to be expressed in the tonoplast of the large central lytic vacuole ( LV ) except for one isoform in Arabidopsis that resides in the plasma membrane . However , plant cells often contain more than one type of vacuole that coexist in the same cell . We recently showed that two TPK isoforms ( OsTPKa and OsTPKb ) from Oryza sativa localise to different vacuoles with OsTPKa predominantly found in the LV tonoplast and OsTPKb primarily in smaller compartments that resemble small vacuoles ( SVs ) . Our study further revealed that it is the C-terminal domain that determines differential targeting of OsTPKa and OsTPKb . Three C-terminal amino acids were particularly relevant for targeting TPKs to their respective endomembranes . In this addendum we further evaluate how the different localisation of TPKa and TPKb impact on their physiological role and how TPKs provide a potential tool to study the physiology of different types of vacuole .
Matching Sentences: [ Sen. 8, subscore: 1.00 ]: In this addendum we further evaluate how the different localisation of TPKa and TPKb impact on their physiological role and how TPKs provide a potential tool to study the physiology of different types of vacuole .
Supplemental links/files: reference in endnote online text related articles pubmed citation