scholarly journals NKG2-C Type II Integral Membrane Protein

2020 ◽  
Author(s):  
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Type Ii

scholarly journals Herpes Simplex Virus 2 UL45 Is a Type II Membrane Protein

1998 ◽  
Vol 72 (5) ◽  
pp. 4430-4433 ◽  
Author(s):  
Adam S. Cockrell ◽  
Martin I. Muggeridge
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Type Ii ◽  
Glycosylation Sites ◽  
Infected Cells ◽  
Membrane Spanning ◽  
Simplex Virus ◽  
Herpes Simplex Virus 2

ABSTRACT In addition to eleven glycoproteins, the herpes simplex virus type 2 (HSV-2) genome encodes several proteins with potential membrane-spanning segments but no asparagine-linked carbohydrates. One of these is UL45. Fractionation of infected cells showed that HSV-2 UL45 is an integral membrane protein, and analysis of UL45 mutants with potential glycosylation sites showed that it has a type II membrane orientation, the first HSV protein known to have this orientation. Furthermore, it is detectable in infected cells at a time similar to that when glycoproteins gB and gD are detected, consistent with a role in cell-cell fusion, which has previously been found for HSV-1 UL45.

scholarly journals The 17-residue transmembrane domain of beta-galactoside alpha 2,6-sialyltransferase is sufficient for Golgi retention

1992 ◽  
Vol 117 (2) ◽  
pp. 245-258 ◽  
Author(s):  
SH Wong ◽  
SH Low ◽  
W Hong
Keyword(s):  
Golgi Apparatus ◽  
Membrane Protein ◽  
Transmembrane Domain ◽  
Integral Membrane Protein ◽  
Chimeric Proteins ◽  
Type Ii ◽  
Lectin Affinity Chromatography ◽  
Golgi Retention ◽  
A Cell ◽  
Golgi Network

beta-Galactoside alpha 2,6-sialyltransferase (ST) is a type II integral membrane protein of the Golgi apparatus involved in the sialylation of N-linked glycans. A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. Lectin affinity chromatography of chimeric proteins bearing this 17-residue sequence suggests that these chimeric proteins are localized in the trans-Golgi cisternae and/or trans-Golgi network. Further experiments suggest that this 17-residue sequence functions as a retention signal for the Golgi apparatus.

Expression and regulation of type II integral membrane protein family members in mouse male reproductive tissues

Endocrine ◽  
2007 ◽  
Vol 31 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Deivendran Rengaraj ◽  
Fei Gao ◽  
Xiao-Huan Liang ◽  
Zeng-Ming Yang
Keyword(s):  
Membrane Protein ◽  
Family Members ◽  
Integral Membrane Protein ◽  
Protein Family ◽  
Type Ii ◽  
Reproductive Tissues

scholarly journals Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein.

1997 ◽  
Vol 8 (6) ◽  
pp. 1073-1087 ◽  
Author(s):  
A D Linstedt ◽  
A Mehta ◽  
J Suhan ◽  
H Reggio ◽  
H P Hauri
Keyword(s):  
Membrane Protein ◽  
Coiled Coil ◽  
Integral Membrane Protein ◽  
Retention Mechanism ◽  
Type Ii ◽  
Golgi Stack ◽  
Chloroquine Treatment ◽  
Retrieval Mechanism ◽  
Endocytotic Vesicles ◽  
Lumenal Domain

It is thought that residents of the Golgi stack are localized by a retention mechanism that prevents their forward progress. Nevertheless, some early Golgi proteins acquire late Golgi modifications. Herein, we describe GPP130 (Golgi phosphoprotein of 130 kDa), a 130-kDa phosphorylated and glycosylated integral membrane protein localized to the cis/medial Golgi. GPP130 appears to be the human counterpart of rat Golgi integral membrane protein, cis (GIMPc), a previously identified early Golgi antigen that acquires late Golgi carbohydrate modifications. The sequence of cDNAs encoding GPP130 indicate that it is a type II membrane protein with a predicted molecular weight of 81,880 and an unusually acidic lumenal domain. On the basis of the alignment with several rod-shaped proteins and the presence of multiple predicted coiled-coil regions, GPP130 may form a flexible rod in the Golgi lumen. In contrast to the behavior of previously studied type II Golgi proteins, overexpression of GPP130 led to a pronounced accumulation in endocytotic vesicles, and endogenous GPP130 reversibly redistributed to endocytotic vesicles after chloroquine treatment. Thus, localization of GPP130 to the early Golgi involves steps that are saturable and sensitive to lumenal pH, and GPP130 contains targeting information that specifies its return to the Golgi after chloroquine washout. Given that GIMPc acquires late Golgi modifications in untreated cells, it seems likely that GPP130/GIMPc continuously cycles between the early Golgi and distal compartments and that an unidentified retrieval mechanism is important for its targeting.

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